Ribosomes:Incredible cycle of birth, fall and survival, Diwali bonus blast by RIL, Nobel rooted at home |
Ramakrishnan's teacher says the spark was there even during college days
The Associated Press Video: 2 Americans Share Nobel Chemistry Prize The Associated Press 
Email this storyIndia-born scientist wins Nobel Prize in Chemistry
The Associated Press Video: 2 Americans Share Nobel Chemistry Prize The Associated Press 
Venky loves to interact with students
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Venky – researcher who solved mystery of proteins
Indian-American Venkatraman Ramakrishnan or just Venky to friends and relatives may have migrated to the US long back, but on Wednesday made a billion people back home proud by winning the Nobel Prize for Chemistry for his pioneering work on ribosome, a cellular `factory' that manufactures proteins that make life tick.
Venky, 57, born in the temple town of Chidambaram in Tamil Nadu, is the seventh Indian or of Indian origin to win the prestigious award.
Born in 1952, Ramakrishnan earned his B.Sc. in Physics (1971) from Baroda University in Gujarat and later migrated to the US to continue his studies where he later got settled and attained US citizenship.
He earned his Ph.D in Physics from Ohio University in the US and later worked as a graduate student at the University of California from 1976-78.
During his stint at the varsity, Ramakrishnan conducted a research with Dr Mauricio Montal, a membrane biochemist and later designed his own 2-year transition from physics to biology.
As a postdoctoral fellow at Yale University, he worked on a neutron-scattering map of the small ribosomal subunit of E Coli. He has been studying ribosome structure ever since.
Ramakrishnan, now a senior scientist at the MRC Laboratory of Molecular Biology in Cambridge has authored several important papers in academic journals.
Coimbatore: Director General of the Central Reserve Police Force, A.S. Gill, said that four new commando battalions will be added to the paramilitary forces especially to fight left wing extremism, giving rise to speculation that Home Ministry is preparing ground for a full blown war against Naxals.
Mueller wins Nobel literary prize | |
German author Herta Mueller has been awarded the 2009 Nobel Prize for Literature, the academy in Stockholm has announced. The Romanian-born writer follows last year's French winner Jean-Marie Gustave Le Clezio, while British writer Doris Lessing won in 2007. Mueller, born in 1953, is renowned for her depiction of the harsh conditions under Nicolae Ceausescu's regime. The Swedish academy praised Mueller for both her poetry and prose. Literary prizes It said the writer had an ability to "depict the landscape of the dispossessed". Mueller was born to a family from Romania's German minority and her mother was deported to a labour camp in the Soviet Union after World War II. She emigrated to Germany in 1987, after being dismissed from her job in Romania during the 1970s due to her refusal to co-operate with the regime's secret police. Her first collection of German language short stories, published in 1982, were censored in Romania. Mueller's initial works were smuggled out of the country, while in later years she was awarded several literary prizes, including Dublin's Impac Award in 1998. One of her later works, 2001's The Appointment, gives great detail about living in a stagnated dictatorship. The writer is awarded a prize of 10 million Swedish Krone (£892,000) along with the honour, which will be presented at a ceremony in Stockholm later this year.
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Horror because the 30-year-old woman from Orissa had just delivered a child in the train toilet and it had slipped through the hole and fallen on the tracks.
The pleasant surprise?
The mother survived after the leap, with a few scratches. Her child survived too, without a scratch.
Rinku, in her final month of pregnancy, was travelling with her husband on the Tata-Chhapra Express.
The couple from Sundergarh district in Orissa were going to Jhajha in Bihar to visit relatives. Their four-year-old daughter was also with them.
Thsi is the RHETORIC of an INDIAN RIBOSOME story which Predestine the Incredible Life Cycle and Aboriginal Indigenous Black Untouchable life in BIOLOGICAL Sustenance without any Social, National, Cultural or Economic Identity. The Nobel Rooted Home makes screaming headlines but it remains always COINCIDENCE that the Rooots grow
in BRAIN Drain without any failure. It is the best Bed for Indian RIBOSOME growth!
We developed so fast and faster is the growth so much so that we assume to be latest Nuclear Super power Capable of defeating GlobalRecession with unprecedented RISILIENCE. But the Motherhood and Pregnancy in India is never limited within the Biological sphere and it is intervened by the Manusmriti Rule, pulling back us in Patriarchial Dark Age of Apartheid and Slavery INFINITE where RIL BONUS One to ONE remains the SHINING India and the RURAL Majority Indigenous aboriginal life survives with UNDERDEVELOPED RIBOSOMES DIABETIC subject to Casualty.
But we as a race, habitual to feed on superstitious Blind Nationalism NEVER fail to describe the Calamities as well as Inequality, Injustice and Persecution, torture and repression, ethnic Cleansing and mass Destructionas the DIVINE affairs Spritually Vague and MYSTERIOUS at the same time, SCREAM on the streets right and RIGHT Naked in a COLORFUL CARNIVAL to celebrate the Foreign Recognition like a NOBEL Prize which we NEVER Deserve as we happen to be HABITUAL to DEPRIVE our blood and RIBOSOMES with typical DISCRIMINATION. Those ICONS which we calim to be ROOTED in India, belong to the BRAIN Drain. Provided they stayed back home, would not they finish up living the life of cats and dogs as most of us do!
Post ModernZionist Manusmriti has shaped in as KNOWLEDGE Economy led by AVTARS like Montek Singh Ahluwalia, PRANAB and no one else but the great KAPIL SIBAL!
Top Universities' Dominance under Threat:
2009 Times Higher Education– QS World University Rankings Reveals
LONDON--(BUSINESS WIRE)--Top 200 ranking published today in Times Higher Education. The complete rankings will appear at 00:01 GMT on 9th October at www.topuniversities.com
Now in their 6th edition, the THE – QS World University Rankings received a record level of responses from both the academic community (9,386) and employers (3,281) reflecting the growing importance of the rankings. The results suggest that the dominance of traditionally elite universities is being challenged.
US and UK institutions still dominate the top ten:
- Harvard retains top spot.
- Cambridge moves to 2nd ahead of Yale.
- University College London rises to 4th ahead of Oxford (5th equal with Imperial College)
- Princeton returns to the top ten.
Other insights among the top 100 universities:
- A dramatic fall in the number of North American universities in the top 100, (42 in 2008; 36 in 2009) reflects the growing presence of Asian and European Institutions on the world stage.
- 39 European universities appear in the top 100 (36 in 2008).
- Two more Asian universities rank in the top 100 – 16 institutions in total.
- The top specialist engineering university is École normale supérieure - Paris
- The top specialist social science university is London School of Economics
Nunzio Quacquarelli, Managing Director of QS observes: "Governments and universities are investing to increase their profile and recognition on the international stage as higher education becomes a global industry. Today the THE –QS World University Rankings are used by employers identifying from where to recruit, academics choosing where to work and with whom to form partnerships, and by parents and students looking to make a sound education decision."
| Times Higher Education – QS World University Rankings 2009 | |||||||
| 2009 Rank | 2008 Rank | School Name | Country | ||||
| 1 | 1 | USA | |||||
| 2 | 3 | UK | |||||
| 3 | 2 | USA | |||||
| 4 | 7 | UK | |||||
| 5= | 6 | UK | |||||
| 5= | 4 | UK | |||||
| 7 | 8 | USA | |||||
| 8 | 12 | USA | |||||
| 9 | 9 | USA | |||||
| 10 | 5 | USA | |||||
Source: QS Intelligence Unit (www.topuniversities.com)
© 2009 QS Quacquarelli Symonds Ltd.
Photos/Multimedia Gallery Available: http://www.businesswire.com/cgi-bin/mmg.cgi?eid=6066334&lang=en
However, Higher Education in India has evolved in distinct and divergent streams with each stream monitored by an apex body, indirectly controlled by the Ministry of Human Resource Development. The 415 universities/ institutions, are mostly funded by the state governments. However, there are 24 important universities called Central universities, which are maintained by the Union Government and because of relatively large funding, they have an edge over the others. The engineering education and business schools are monitored and accredited by the All India Council for Technical Education (AICTE) while medical education is monitored and accredited by the Medical Council of India (MCI). Like-wise, agriculture education and research is monitored by the Indian Council for Agriculture Research. Apart from these, National Council for Teacher Education (NCTE) controls all the teacher training institutions in the country. The country has some ace engineering, management and medical education institutions which are directly funded by the Ministry of Human Resource Development of the Union Government. Admission to all professional education colleges is done through all-India common admission tests of which the IIT-JEE, AIEEE, CAT and CPMT are the most popular ones. Most of the institutions reserve a small percentage of seats for foreign students. JK gets 2 Central varsities, misses IIM NEW DELHI : Politics had it's ugly effect on Jammu and Kashmir on September 25 as the Central government decided to bless the state with two Central universities but dropped plans to award an Indian Institute of Management to the state. Surprisingly, all the political parties have welcomed the decision, blissfully forgetting the fact that they have lost a gem in the IIM. more Karnataka VCs' panel to monitor university autonomy Common Admission Test makes an online debut Govt revises pay for IIT, IIM faculty NCHER proposal gets prime minister's nod NEW DELHI : The Human Resource Development Ministry's plan to set up a National Commission for Higher Education and Research (NCHER) to replace existing regulatory bodies like UGC and AICTE is understood to have got support from Prime Minister Manmohan Singh. more Sikkim Manipal Inst closed after clash GUWAHATI : Bitter clashes between the boarders and day scholars forced the management of Sikkim Manipal Institute of Technology (SMIT) in Mazitar to shut the institute indefinitely, asking the boarders to leave for home.
:: TOP STORIES ::
Law soon to ban capitation fee, says Kapil Sibal
NEW DELHI : The Ministry of Human Resource Development drafted a tough law to banish capitation fee, check malpractices by private institutions and to monitor their activities, says a PTI report. more
BANGALORE : On September 3 Karnataka Governor-Chancellor R Bhardwaj appointed a five-member committee headed by University Vice-Chancellor S Sherigara to monitor university autonomy. more
Planning Commission approves 20 more IIITs for country
NEW DELHI : Planning Commission has given its 'in principle' approval to Ministry of Human Resource Development's proposal to set up 20 new lllTs through Public Private Partnership (PPP). more
LUCKNOW : Registration for Common Admission Test (CAT) 2009 opened on September 9 with thousands filling up the online form. The process was smooth on day one but students voiced concern. more
:: KEY STORIES :: 
MAMTA scraps railway chair at iim ahemdabad
PRESIDENCY COLLEGE STUDENTS PRESS FOR AUTONOMY
PANEL TO ADJUDICATE ON IIT DISPUTES FORMED
KANPUR IIT STUDENTS DEVELOP NANO SATELLITE
MHRD SACKS JAMSHEDPUR NIT OFFICIATING DIRECTOR
NEW DELHI : Human Resource Development Ministry has revised controversial pay scales for IIT and IIM teachers, increasing salaries for assistant professors but ignoring other key demands and bypassing the Union cabinet that approved the contentious regime. The revised pay notification, issued by the ministry late September 16 evening, allows assistant professors to leap into a higher pay range after three years, but is silent on other demands made by teachers. more 
The trouble began over a trivial issue in a volleyball match and culminated into a series of bitter, violent clashes. more
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The 2009 Nobel Prize in Chemistry has been awarded to Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E. Yonath for enlightening the science community on the structure and function of the ribosome, the protein factory of all living organisms. Out of the three big molecules for life (DNA, RNA, and proteins), proteins arguably do most of the work. They provide structural stability to our cells, give us mechanical motion in our muscles, transport the oxygen that we inhale, and play many other key parts in nearly every chemical reaction that occurs in cells.
DNA contains genetic information, but it is essentially a passive set of instructions and designs that cannot accomplish anything on its own. For there to be life, proteins must help transcribe the data in DNA into RNA, another carrier of information that is more chemically active than DNA, but still less functional than proteins. The messages in the RNA are translated in the ribosome to make specific sequences of proteins, which then goes on to perform essential biochemical functions. Thus, in studying the chemistry of life, we must understand how proteins are made in ribosomes.
The three Nobel winners used X-ray crystallography to identify and map the positions of the atoms in the ribosome to give scientists 3D models to examine and dissect for crucial information on the molecular level. This was an impressive feat as there are hundreds of thousands of atoms involved. Their work has benefited many other areas of research, including the study of antibiotics. As making proteins is essential for bacteria survival, the ribosome is a practical target for drugs. Ramakrishnan, Steitz, and Yonath have provided vital information for the design of new antibiotics.
Venkatraman Ramakrishnan obtained his PhD in physics at Ohio University and studied biology at the University of California-San Diego. He is currently a senior research fellow at the MRC Laboratory of Molecular Biology in Trinity College, Cambridge. Among his first contributions to the study of ribosomes, he published a paper in 1981 and two in 1984 on the structure of a subunit of in an E. coli ribosome. From then on, he continued to solve the structures of the many components in the ribosome, and his latest major work was published in Science last year, providing insight on how protein synthesis knows when to end and detach the finished protein.
Thomas Steitz studied at Harvard and graduated with a PhD in 1966. Since then, he has contributed structural studies on a wide range of proteins, from yeast hexokinase to the HIV reverse transcriptase. Notably, he was the first to provide a structure for DNA polymerase, an enzyme involved in replicating DNA. He has also determined the structure of the 50S subunit of a ribosome along with how it interacts with around two dozen antibiotics. Currently, as a professor of Molecular Biophysics and Biochemistry at Yale University, he is directing his research group in capturing structures of the 70S ribosome in its various states.
Ada Yonath, the first Israeli woman and fourth woman overall to win a Nobel Prize in Chemistry, earned her PhD in X-ray crystallography at the Weizmann Institute of Science, where she is now a professor. She published her first crystal structure in 1965 on a sequence of amino acids, the components of proteins. Over the last 44 years, she has steadily published papers on structures of proteins, RNA related to protein synthesis, and subunits of the ribosome, including seven so far this year.
There is no doubt that Ramakrishnan, Steitz, and Yonath are key figures in the continuing work on discovering the function and structure of the ribosome. Their work has influenced every facet of chemistry, from organic synthesis to biophysical research. Of course, their achievements are built on the work of many others, such as Harry Noller at the University of California-Santa Cruz and Peter Moore at Yale University. Noller and Moore have made significant contributions to deciphering the interactions and activities of the ribosome.
LONDON — British and US universities dominate the top of a league table of universities worldwide published Thursday, but Oxford has slipped one place to joint fifth.
Harvard remains in top spot in the Times Higher Education league table, followed by Britain's Cambridge University then Yale in third place, with London's University College and Imperial College in fourth and fifth.
But Asian universities, while still struggling to break into the top 20, are moving upwards, with numbers in the top 200 growing in Japan, Hong Kong, South Korea and Malaysia.
After the University of Tokyo in 22nd place come the University of Hong Kong in 24th, Japan's Kyoto University in 25th, and the National University of Singapore in 30th.
Philip Altbach of Boston University says the Asian improvement is due to a number of factors.
"These countries have invested heavily in higher education in recent years, and this is reflected in the improved quality in their top institutions," he told the Times education weekly.
"They have also attempted to internationalise their universities by hiring more faculty from overseas... this helps to improve their visibility globally," he added.
Europe's top non-British university is Switzerland's Federal Institute of Technology in 20th spot, followed by France's Ecole Normale Superieure in 28th. The top German university is the Technical University of Munich, in 55th.
The top non-US and non-European universities are the Australian National University in 17th place, down one, and Canada's McGill University in 18th position, down two.
India third in global Muslim population of 1.57 bn
October 8th, 2009
WASHINGTON - The Muslim population in the world stands at 1.57 billion, and India has the third largest number of Muslims at over 160 million after Indonesia and Pakistan.
Muslims constitute 23 percent of the 6.8 billion global population, according to a new study in 232 countries and territories. Indonesia and Pakistan are home to over 200 million and 174 million Muslims.
"The new study is based on the best available data," said the Forum on Religion and Public Life, a unit of US-based think tank Pew Research Centre, which conducted the study.
"Previously published estimates of the size of the global Muslim population have ranged widely from 1 billion to 1.8 billion," said the centre, which analysed over 1,500 sources, including census reports, demographic studies and general population surveys.
India is home to 160.95 million Muslims, representing 13.4 percent of the country's population, or 10.3 percent of their global numbers.
India also tops the list of countries with the largest number of Muslims living as a minority community. India is one of four countries accounting for most of the global Shia population.
The key findings of the study, released here late Wednesday, are:
- India has the third largest population of Muslims worldwide
- China has more Muslims than Syria
- Russia is home to more Muslims than Jordan and Libya combined
- While Muslims are found on all five inhabited continents, more than 60 percent of the global Muslim population is in Asia
- Middle East and North Africa account for 20 percent of the Muslim population
- The Middle East-North Africa region has the highest percentage of Muslim-majority countries
- More than half of the 20 countries and territories in Middle East-North Africa region have populations that are approximately 95 percent Muslim or more
- More than 300 million Muslims, or a fifth of the world's Muslim population, live in countries where Islam is not the majority religion
- These minority Muslim populations are often quite large
- Of the total Muslim population, 10-13 percent are Shias and 87-90 percent are Sunnis
- Most Shias, between 68-80 percent, live in just four countries, namely Iran, Pakistan, India and Iraq
The new report has an executive summary, maps and charts to illustrate the geographic distribution of Muslims, explanations of the study's methodologies and a list of data sources by country.
Indonesia accounts for the largest number of Muslims at 202.87 million, or 88.2 percent of the country's population, followed by Pakistan with 174.08 million, or 96.3 percent of the population.
Bangladesh, Egypt, Nigeria, Iran, Turkey, Algeria and Morocco, in that order, make up the 10 countries with the largest population of Muslims.
Earlier today, the 2009 Nobel Prize in Chemistry was awarded to:
- Venkatraman Ramakrishnan, MRC Laboratory of Molecular Biology, Cambridge,United Kingdom
- Thomas A. Steitz, Yale University, New Haven, CT, USA
- Ada E. Yonath, Weizmann Institute of Science, Rehovot, Israel
"for studies of the structure and function of the ribosome."
These scientists used a method called X-ray crystallography to map the position for each and every one of the hundreds of thousands of atoms that make up the ribosome.
But, what is a ribosome?
Ribosomes are cellular structures that produce proteins. DNA contains the informational "blueprint" for proteins, but ribosomes are the structures that actually make proteins. There are tens of thousands of proteins in the body and they all have different forms and functions. Essentially, poteins build and control life at the chemical level.
Thanks to the work of these three scientists, we now have a more detailed understanding of how ribosomes function. Specifically, they researched how different antibiotics bind to ribosomes. After all, if an antibiotic can be designed to specifically bind to –and impair function of –the ribosomes of a bacteria, the bacteria cell will die.
This information is now being used by scientists in order to develop new antibiotics, directly assisting the saving of lives and decreasing humanity's suffering.
Source: Nobelprize.org
Read more: http://www.greenpacks.org/2009/10/07/2009-nobel-prize-in-chemistry-what-is-a-ribosome/#ixzz0TLKUgoKS
Ribosome
From Wikipedia, the free encyclopedia
Organelles:
(1) nucleolus
(2) nucleus
(3) ribosomes (little dots)
(4) vesicle
(5) rough endoplasmic reticulum (ER)
(6) Golgi apparatus
(7) Cytoskeleton
(8) smooth ER
(9) mitochondria
(10) vacuole
(11) cytoplasm
(12) lysosome
(13) centrioles within centrosome
Ribosomes (from ribonucleic acid and "Greek: soma (meaning body)") are complexes of RNA and protein that are found in all cells with nuclei. The ribosome is part of the mechanism that translates the DNA sequence into the protein sequence (proteins are translated from mRNA, mRNA is transcribed from DNA, so DNA is not 'translated' directly into protein). Ribosomes from bacteria, archaea and eukaryotes (the three domains of life on Earth), have significantly different structure and RNA. The ribosomes in the mitochondria of eukaryotic cells resemble those in bacteria, reflecting the evolutionary origin of this organelle.[1]
The ribosome is part of the mechanism that translates the genetic code from nucleic acid into protein chains. Ribosomes assemble individual amino acids into polypeptide chains. Ribosomes bind to a messenger RNA molecule, which they use as a template to join the correct sequence of amino acids. The amino acids are attached to transfer RNA molecules, which read the messenger RNA sequence and attach the proteins in the correct sequence.
Contents[hide] |
[edit] Description
Ribosomes are about 20 nm (200 ångströms) in diameter and are composed of 65% ribosomal RNA and 35% ribosomal proteins (known as a ribonucleoprotein or RNP)[citation needed]. They translate messenger RNA (mRNA) to build polypeptide chains (e.g., proteins) using amino acids delivered by transfer RNA (tRNA). Their active sites are made of RNA, so ribosomes are now classified as "ribozymes".[2]
Ribosomes build proteins from the genetic instructions held within messenger RNA. Free ribosomes are suspended in the cytosol (the semi-fluid portion of the cytoplasm); others are bound to the rough endoplasmic reticulum, giving it the appearance of roughness and thus its name, or to the nuclear envelope. As ribozymes are partly constituted from RNA, it is thought that they might be remnants of the RNA world.[3] Although catalysis of the peptide bond involves the C2 hydroxyl of RNA's P-site adenosine in a protein shuttle mechanism, other steps in protein synthesis (such as translocation) are caused by changes in protein conformations.
Ribosomes are sometimes referred to as organelles, but the use of the term organelle is often restricted to describing sub-cellular components that include a phospholipid membrane, which ribosomes, being entirely particulate, do not. For this reason, ribosomes may sometimes be described as "non-membranous organelles".
Ribosomes were first observed in the mid-1950s by Romanian cell biologist George Palade using an electron microscope as dense particles or granules[4] for which he would win the Nobel Prize. The term "ribosome" was proposed by scientist Richard B. Roberts in 1958:
During the course of the symposium a semantic difficulty became apparent. To some of the participants, "microsomes" mean the ribonucleoprotein particles of the microsome fraction contaminated by other protein and lipid material; to others, the microsomes consist of protein and lipid contaminated by particles. The phrase "microsomal particles" does not seem adequate, and "ribonucleoprotein particles of the microsome fraction" is much too awkward. During the meeting the word "ribosome" was suggested; this seems a very satisfactory name, and it has a pleasant sound. The present confusion would be eliminated if "ribosome" were adopted to designate ribonucleoprotein particles in sizes ranging from 35 to 100S.
– Roberts, R. B., Microsomal Particles and Protein Synthesis[5]
The structure and function of the ribosomes and associated molecules, known as the translational apparatus, has been of research interest since the mid-twentieth century and is a very active field of study today.
Ribosomes consist of two subunits (Figure 1) that fit together (Figure 2) and work as one to translate the mRNA into a polypeptide chain during protein synthesis (Figure 3). Bacterial subunits consist of one or two and eukaryotic of one or three very large RNA molecules (known as ribosomal RNA or rRNA) and multiple smaller protein molecules. Crystallographic work has shown that there are no ribosomal proteins close to the reaction site for polypeptide synthesis. This suggests that the protein components of ribosomes act as a scaffold that may enhance the ability of rRNA to synthesize protein rather than directly participating in catalysis (See: Ribozyme).
[edit] Biogenesis
In bacterial cells, ribosomes are synthesized in the cytoplasm through the transcription of multiple ribosome gene operons. In eukaryotes, the process takes place both in the cell cytoplasm and in the nucleolus, which is a region within the cell nucleus. The assembly process involves the coordinated function of over 200 proteins in the synthesis and processing of the four rRNAs, as well as assembly of those rRNAs with the ribosomal proteins.
[edit] Ribosome locations
Ribosomes are classified as being either "free" or "membrane-bound".
Free and membrane-bound ribosomes differ only in their spatial distribution; they are identical in structure and function. Whether the ribosome exists in a free or membrane-bound state depends on the presence of an ER-targeting signal sequence on the protein being synthesized.
[edit] Free ribosomes
Free ribosomes are free to move about anywhere in the cytosol. Proteins that are formed from free ribosomes are used within the cell. Proteins containing disulfide bonds using cysteine amino acids cannot be produced outside of the lumen of the endoplasmic reticulum.
[edit] Membrane-bound ribosomes
When certain proteins are synthesized the ribosome making this protein can become "membrane-bound". In eukaryotic cells this happens in a region of the endoplasmic reticulum (ER) called the "rough ER". The newly produced polypeptide chains are inserted directly into the ER by the ribosome and are then transported to their destinations. Bound ribosomes usually produce proteins that are used within the cell membrane or are expelled from the cell via exocytosis.
[edit] Structure
The ribosomal subunits of prokaryotes and eukaryotes are quite similar.[7]
The unit of measurement is the Svedberg unit, a measure of the rate of sedimentation in centrifugation rather than size and accounts for why fragment names do not add up (70S is made of 50S and 30S).
Prokaryotes have 70S ribosomes, each consisting of a small (30S) and a large (50S) subunit. Their large subunit is composed of a 5S RNA subunit (consisting of 120 nucleotides), a 23S RNA subunit (2900 nucleotides) and 34 proteins. The 30S subunit has a 1540 nucleotide RNA subunit (16S) bound to 21 proteins.[7]
Eukaryotes have 80S ribosomes, each consisting of a small (40S) and large (60S) subunit. Their large subunit is composed of a 5S RNA (120 nucleotides), a 28S RNA (4700 nucleotides), a 5.8S subunit (160 nucleotides) and ~49 proteins. The 40S subunit has a 1900 nucleotide (18S) RNA and ~33 proteins.[7]
The ribosomes found in chloroplasts and mitochondria of eukaryotes also consist of large and small subunits bound together with proteins into one 70S particle.[7] These organelles are believed to be descendants of bacteria (see Endosymbiotic theory) and as such their ribosomes are similar to those of bacteria.[8]
The various ribosomes share a core structure, which is quite similar despite the large differences in size. The extra RNA in the larger ribosomes is in several long continuous insertions, such that they form loops out of the core structure without disrupting or changing it.[7] All of the catalytic activity of the ribosome is carried out by the RNA, the proteins reside on the surface and seem to stabilize the structure.[7]
The differences between the bacterial and eukaryotic ribosomes are exploited by pharmaceutical chemists to create antibiotics that can destroy a bacterial infection without harming the cells of the infected person. Due to the differences in their structures, the bacterial 70S ribosomes are vulnerable to these antibiotics while the eukaryotic 80S ribosomes are not.[9] Even though mitochondria possess ribosomes similar to the bacterial ones, mitochondria are not affected by these antibiotics because they are surrounded by a double membrane that does not easily admit these antibiotics into the organelle.[10]
[edit] High-resolution structure
The general molecular structure of the ribosome has been known since the early 1970s. In the early 2000s the structure has been achieved at high resolutions, in the order of a few ångströms.
The first papers giving the structure of the ribosome at atomic resolution were published in rapid succession in late 2000. First, the 50S (large bacteria) subunit from the archea, Haloarcula marismortui was published.[11] Soon after the structure of the 30S subunit from Thermus thermophilus was published.[6] Shortly thereafter a more detailed structure was published.[12] Early the next year (May 2001) these coordinates were used to reconstruct the entire T. thermophilus 70S particle at 5.5 ångström resolution.[13]
Two papers were published in November 2005 with structures of the Escherichia coli 70S ribosome. The structures of vacant ribosome were determined at 3.5-ångström resolution using x-ray crystallography.[14] Then, two weeks later, a structure based on cryo-electron microsopy was published,[15] which depicts the ribosome at 11-15 ångström resolution in the act of passing a newly synthesized protein strand into the protein-conducting channel.
First atomic structures of the ribosome complexed with tRNA and mRNA molecules were solved by using X-ray crystallography by two groups independently, at 2.8 ångström[16] and at 3.7 ångström.[17] These structures allow one to see the details of interactions of the Thermus thermophilus ribosome with mRNA and with tRNAs bound at classical ribosomal sites. Interactions of the ribosome with long mRNAs containing Shine-Dalgarno sequences were visualized soon after that at 4.5- to 5.5-ångström resolution.[18]
[edit] Function
Ribosomes are the workhorses of protein biosynthesis, the process of translating mRNA into protein. The mRNA comprises a series of codons that dictate to the ribosome the sequence of the amino acids needed to make the protein. Using the mRNA as a template, the ribosome traverses each codon (3 nucleotides) of the mRNA, pairing it with the appropriate amino acid provided by a tRNA. Molecules of transfer RNA (tRNA) contain a complementary anticodon on one end and the appropriate amino acid on the other. The small ribosomal subunit, typically bound to a tRNA containing the amino acid methionine, binds to an AUG codon on the mRNA and recruits the large ribosomal subunit. The ribosome then contains three RNA binding sites, designated A, P, and E. The A site binds an aminoacyl-tRNA (a tRNA bound to an amino acid); the P site binds a peptidyl-tRNA (a tRNA bound to the peptide being synthesized); and the E site binds a free tRNA before it exits the ribosome. Protein synthesis begins at a start codon AUG near the 5' end of the mRNA. mRNA binds to the P site of the ribosome first. The ribosome is able to identify the start codon by use of the Shine-Dalgarno sequence of the mRNA in prokaryotes and Kozak box in eukaryotes.
In Figure 3, both ribosomal subunits (small and large) assemble at the start codon (towards the 5' end of the mRNA). The ribosome uses tRNA that matches the current codon (triplet) on the mRNA to append an amino acid to the polypeptide chain. This is done for each triplet on the mRNA, while the ribosome moves towards the 3' end of the mRNA. Usually in bacterial cells, several ribosomes are working parallel on a single mRNA, forming what is called a polyribosome or polysome.
[edit] Nobel Prize
The Nobel Prize in Chemistry 2009 was awarded to Drs Venkatraman Ramakrishnan, Thomas A. Steitz and Ada E. Yonath "for studies of the structure and function of the ribosome"[19]
[edit] See also
[edit] References
- ^ Benne R, Sloof P (1987). "Evolution of the mitochondrial protein synthetic machinery". BioSystems 21 (1): 51–68. doi:. PMID 2446672.
- ^ Rodnina MV, Beringer M, Wintermeyer W (2007). "How ribosomes make peptide bonds". Trends Biochem. Sci. 32 (1): 20–6. doi:. PMID 17157507.
- ^ Cech T (2000). "Structural biology. The ribosome is a ribozyme". Science 289 (5481): 878–9. doi:. PMID 10960319.
- ^ G.E. Palade. (1955) "A small particulate component of the cytoplasm". J Biophys Biochem Cytol. Jan;1(1): pages 59-68. PMID 14381428
- ^ Roberts, R. B., editor. (1958) "Introduction" in Microsomal Particles and Protein Synthesis. New York: Pergamon Press, Inc.
- ^ a b Schluenzen F, Tocilj A, Zarivach R, Harms J, Gluehmann M, Janell D, Bashan A, Bartels H, Agmon I, Franceschi F, Yonath A (2000). "Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution". Cell 102 (5): 615–23. doi:. PMID 11007480.
- ^ a b c d e f The Molecular Biology of the Cell, fourth eddition. Bruce Alberts, et al. Garland Science (2002) pg. 342 ISBN 0-8153-3218-1
- ^ The Molecular Biology of the Cell, fourth edition. Bruce Alberts, et al. Garland Science (2002) pg. 808 ISBN 0-8153-3218-1
- ^ Recht MI, Douthwaite S, Puglisi JD (1999). "Basis for bacterial specificity of action of aminoglycoside antibiotics". EMBO J 18 (11): 3133–8. doi:. PMID 10357824.
- ^ O'Brien, T.W., The General Occurrence of 55S Ribosomes in Mammalian Liver Mitochondria. J. Biol. Chem., 245:3409 (1971).
- ^ a b Ban N, Nissen P, Hansen J, Moore P, Steitz T (2000). "The complete atomic structure of the large ribosomal subunit at 2.4 ångström resolution". Science 289 (5481): 905–20. doi:. PMID 10937989.
- ^ Wimberly BT, Brodersen DE, Clemons WM Jr, Morgan-Warren RJ, Carter AP, Vonrhein C, Hartsch T, Ramakrishnan V. Structure of the 30S ribosomal subunit. Nature. 2000 Sep 21;407(6802):327-39. PMID 11014182
- ^ Yusupov MM, Yusupova GZ, Baucom A, Lieberman K, Earnest TN, Cate JH, Noller HF. Crystal structure of the ribosome at 5.5 ångström resolution. Science. 2001 May 4;292(5518):883-96. Epub 2001 Mar 29. PMID 11283358
- ^ Schuwirth BS, Borovinskaya MA, Hau CW, Zhang W, Vila-Sanjurjo A, Holton JM, Cate JH. Structures of the bacterial ribosome at 3.5 ångström resolution. Science. 2005 Nov 4;310(5749):827-34. PMID 16272117
- ^ Mitra K, Schaffitzel C, Shaikh T, Tama F, Jenni S, Brooks CL 3rd, Ban N, Frank J. Structure of the E. coli protein-conducting channel bound to a translating ribosome. Nature. 2005 Nov 17;438(7066):318-24. PMID 16292303
- ^ Selmer, M., Dunham, C.M., Murphy, F.V IV, Weixlbaumer, A., Petry S., Kelley, A.C., Weir, J.R. and Ramakrishnan, V. (2006). Structure of the 70S ribosome complexed with mRNA and tRNA. Science , 313, 1935-1942. PMID 16959973
- ^ Korostelev A, Trakhanov S, Laurberg M, Noller HF. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell. 2006 Sep 22;126(6):1065-77
- ^ Yusupova G, Jenner L, Rees B, Moras D, Yusupov M. Structural basis for messenger RNA movement on the ribosome. Nature. 2006 Nov 16;444(7117):391-4
- ^ 2009 Nobel Prize in Chemistry, Nobel Foundation.
[edit] External links
- 70S Ribosome Architecture Animation of a working ribosome. Requires the Chime browser plugin from this site (where registration is required).
- Lab computer simulates ribosome in motion
- Role of the Ribosome, Gwen V. Childs, copied here
- Molecule of the Month © RCSB Protein Data Bank:
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This article contains material from the Science Primer published by the NCBI, which, as a U.S. government publication, is in the public domain.
| Incredible cycle of birth, fall and survival | ||
| AMIT UKIL AND OUR BUREAU | ||
Purulia, Oct. 7: Call it providence or a pleasant surprise, but it was horror that made Rinku Devi Rai leap out of a running train last night. Horror because the 30-year-old woman from Orissa had just delivered a child in the train toilet and it had slipped through the hole and fallen on the tracks. The pleasant surprise? The mother survived after the leap, with a few scratches. Her child survived too, without a scratch. Rinku, in her final month of pregnancy, was travelling with her husband on the Tata-Chhapra Express. The couple from Sundergarh district in Orissa were going to Jhajha in Bihar to visit relatives. Their four-year-old daughter was also with them. Around 10 last night, Rinku went to the toilet in their general compartment to relieve herself. In what seems to be a case of precipitate labour, Rinku delivered a child sitting in the toilet. Lying in a hospital bed, Rinku recounted that as she squatted in the toilet, "there was a mild pain". To her surprise "the baby came out, chord, placenta and all". "But before I could realise what had happened, it slipped through the hole. I became hysterical, came out of the toilet and jumped from the train," she said. She was shouting incoherently as she jumped, husband Bhola said later. Co-passengers thought Rinku had committed suicide and began shouting. A scared Bhola pulled the chain. By then, the train, though travelling at a slow speed, had already moved almost half a kilometre. Bhola and the other passengers got off and ran down the tracks. They found Rinku, sitting by the tracks, the baby in her arms. "Much later she realised that we have a boy," Bhola said, laughing. The engine driver, in the meantime, had sent a radio message to the nearest signal cabin. The message was passed on to the control room at Adra as the train was about to enter that division. The control room informed S.P. Majumdar, the station master in Purulia. "We were ready with a doctor and a nurse at the station when the train came in at 11.15pm. After preliminary examination and first aid, they were taken to the Deben Mahato District Hospital in Purulia," Majumdar said. "The mother had a few scratches on her left arm. And the baby, nothing at all. Really fortuitous." Majumdar later said the train was moving at a slow speed, about 15kmph as it was passing a halt between Gamaria and Birajpur stations in Jharkhand. "This increased the survival chances of the baby and the mother," he said. Hospital superintendent Swapan Sarkar said cases of delivery like Rinku's are called precipitate labour. "It is not common. It can happen even while the mother is walking. Rinku's baby was not pre-term. She said her date of delivery was October 21." The mother and the child were doing fine, Sarkar added. Purulia station master Majumdar asked Rinku: "After all this, what will you call your boy?" Then he himself suggested: "Call him Duronto (restless). Look how he scampered off immediately after birth." At the Purulia hospital, a nurse suggested another name: Mrityunjay (one who conquers death). Rinku and Bhola haven't made up their mind yet. But will they take the same train again? Bhola, a small businessman, smiled and said: "We plan to take the same express to Bihar after the eventful break in our journey." |
| Nobel rooted at home - Chemistry prize for Indian American | |
| AMIT ROY IN LONDON AND G.S. MUDUR IN BERLIN | |
Oct. 7: Venkatraman Ramakrishnan thought it was a joke, especially the Swedish accent. The Indian-born US citizen, who graduated from Baroda, had just been told over the phone that he had won the Chemistry Nobel, by a caller claiming to be from the Swedish Academy. "Well, you know, I thought it was an elaborate joke. I have friends who play practical jokes," the scientist, "Venky" to his friends, said from his lab in Cambridge, Britain. "I complimented him on his Swedish accent." But the 57-year-old who loves sugarcane juice was in for a sweet surprise: he had indeed won the prize, jointly with Yale professor Thomas Steitz and Israel's Ada Yonath. They had all independently mapped, atom by atom, the cell's protein-making factories or ribosomes by using X-ray crystallography. Their feat has spurred the development of new antibiotics, thus "directly assisting the saving of lives and decreasing humanity's suffering", the academy said. The Indian is senior scientist and group leader at the Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge — the same lab where James Watson and Francis Crick mapped the DNA's double-helix structure in 1953, a year after Ramakrishnan was born in Chidambaram, Tamil Nadu. His work builds on Darwin's theory of evolution and, more directly, on the work of Watson, Crick and Maurice Wilkins, who won the 1962 Nobel. Ribosomes produce the proteins whose sequence in the DNA forms the blueprint for life and controls the chemistry of all living beings. Ramakrishnan is a fellow at Trinity College, which links him to another Indian Nobel laureate, Amartya Sen. A joke has it that a stone flung into Trinity is likely to fall on a Nobel winner. Tamil Nadu has now caught up with Bengal in the Nobel stakes — with a little help from America. It has Ramakrishnan, Subrahmanyan Chandrasekhar and C.V. Raman to pit against Tagore, Sen and Mother Teresa. Bengal, though, can argue that J.C. Bose and Satyen Bose undoubtedly deserved the prize, that Raman did his pioneering work in Calcutta, and that Bangladeshi Peace Nobel winner Muhammad Yunus is a Bengali. "I have to say I am deeply indebted to all of the brilliant associates, students and post-docs who worked in my lab…" Ramakrishnan said modestly. "Well, I'll be honest with you. I was a theoretical physicist but my PhD work was on a problem that was not particularly interesting to me at the time. And I used to subscribe to Scientific American and found that there were all these wonderful discoveries happening in biology…. So, I decided to switch." Ramakrishnan said that because he had been inundated by calls in a laboratory, he was not able to break the news immediately to his own family. "It looks like, from the way the phone's ringing, that today's going to be written off. But I haven't even told my wife yet. I couldn't reach her. She's probably gone for a walk, and she doesn't use a mobile phone, so it will be interesting." "He is a fantastic person —very popular among students and faculty here," said Umesh Varshney, professor at IISc Bangalore, where Ramakrishnan spent a little over two weeks last December. "He can talk to you at exactly the right wavelength, whether you're a senior faculty member or a young student," Varshney said, recalling how Ramakrishnan would visit a local stall to gulp down sugarcane juice. The Nobel trio will split the $1.4 million (Rs 6.56 crore). Their work, which shows how some antibiotics block the bacterial ribosomes, may help tame drug-resistant bacteria and minimise the side effects of antibiotics. Yonath said the trio were competitors but "we meet a lot… so there's a lot of interaction, and not always negative." | |
| WITH AP AND REUTERS INPUTS |
| Diwali bonus blast by RIL | |
| OUR SPECIAL CORRESPONDENT | |
Mumbai, Oct. 7: Reliance Industries Ltd (RIL), India's largest private company, stunned the markets today with an offer of bonus shares in the ratio of 1:1 to its 35 lakh shareholders. RIL is coming out with a bonus issue after a gap of 12 years and this is only the third time in its 34-year history that it has rewarded its shareholders with free shares. Back in 1997, it had offered a similar one-for-one bonus. Mukesh Ambani, chairman of RIL, has consistently fobbed off pressure from shareholders to issue bonus shares over the past few years. But he finally came up with a gift-wrapped package of about 164 crore free shares just 10 days before Diwali. The bonus issue will rank among the biggest issue of free shares in India's corporate history. "It (the bonus announcement) was completely unexpected," said Arun Kejriwal, director, KRIS, who is also an RIL shareholder. The RIL announcement was made after market hours. Earlier, the stock had closed lower by 1.6 per cent at Rs 2,099 on the BSE but market mavens expect it to soar tomorrow. Kejriwal said the bonus announcement would provide strong support to the sensex. The offer of one free share for every share currently held was approved by the board of directors less than a fortnight before Mukesh Ambani-owned RIL squares off for the final battle with Anil Ambani's Reliance Natural Resources Ltd (RNRL) in the Supreme Court over gas supplies from the Krishna-Godavari basin. The company said the shareholders of erstwhile Reliance Petroleum Ltd (RPL), which has recently been amalgamated with RIL, would also get the bonus shares. Anil Ambani will not benefit from this windfall since he no longer holds shares in RIL after the group formally split. There was icing on the bonus announcement: RIL shareholders will also get an interim dividend of Rs 13 on every share that they hold. The dividend payout will amount to Rs 2,219 crore inclusive of taxes of Rs 322 crore. "The proposal for bonus and dividend continue Reliance's tradition of rewarding shareholders on a sustained basis," RIL said. It added that since the demerger in 2005, RIL had created value of Rs 2,47,000 crore in terms of market capitalisation and shareholders had earned a 40 per cent compounded return. "We had committed to reward our shareholders…" Mukesh Ambani said. |
| First lab: family that valued education |
| K.P. NAYAR |
| Washington, Oct. 7: The phone started ringing at 2am today at the Seattle residence of retired professor C.V. Ramakrishnan. The callers, mostly from American television networks, wanted to speak to Venkatraman Ramakrishnan. Annoyed at being woken up from deep sleep, C.V. Ramakrishnan told the first caller that his son had not been living at this Seattle address for 10 years. "But this is the address from which he renewed his Washington state driving licence," the caller protested. "This is the address on his US passport," the television reporter insisted. C.V. Ramakrishnan, trying to shed the ennui from an abrupt awakening, wondered what it was that the media wanted with his only son at this unearthly hour. Before he could conjure up any answer, the reporter, realising that C.V. Ramakrishnan did not know the big news that had just broken in Europe, told the father that his son, Indian American Venkatraman Ramakrishnan, a professor at Cambridge, had just been announced as one of three winners of the Nobel Prize for Chemistry in 2009. Was this true? Or was this TV reporter trying to trip him up for some other reason? Only for a very fleeting second did C.V. Ramakrishnan have a slight confusion. He quickly recalled that his wife, the late professor R. Rajalakshmi, used to be absolutely confident that one day their son would be awarded the Nobel Prize for his work in biochemistry. Her confidence was not that of a doting parent, who, of course, thought highly of her son. Both Rajalakshmi and her husband were thoroughly familiar with the work that their son was engaged in. Chidambaram, Tamil Nadu-born, Baroda-educated Venkatraman Ramakrishnan comes from a family of biochemists. The family always placed a high premium on education. Rajalakshmi started her career as a high school teacher in Chidambaram, where Coimbatore-born C.V. Ramakrishnan met and married her. Shortly after they married, the husband left for the US for a post-doctoral fellowship at the University of Wisconsin–Madison. Hargobind Khorana, an Indian American Nobel laureate in 1968, was at the University of Wisconsin–Madison when Khorana was awarded the Nobel for medicine. Rajalakshmi, who followed her husband to Canada, where he joined the prestigious National Research Council, enrolled at McGill University for a PhD. Although Rajalakshmi and C.V. Ramakrishnan were doing very well in the West, the pull of the motherland was too strong, even at a time of severe brain drain from India. In 1955, when the University of Baroda invited C.V. Ramakrishnan to join the leading institution of higher learning in Gujarat, the couple gave up their career in north America and returned home. Together, C.V. Ramakrishnan and Rajalakshmi not only set up the biochemistry faculty at the University of Baroda, but also won global recognition for their work on the role of nutrition in brain development. The theories that they developed with generous grants for this pioneering work ran counter to what the West was propagating at that time and helped human development in the Third World. Their young son was then specialising in physics and had already done his BSc. from the University of Baroda and his PhD. later from Ohio University, both in physics. But the family's partiality towards biology and biochemistry eventually overwhelmed him too and the latest Nobel laureate joined Yale as a post-doctoral fellow in the chemistry department. Other similar openings came his way in the US, but Venkatraman Ramakrishnan chose to move to England because Cambridge offered him an escape from uncertainties in the US that come from having to constantly seek grants for research and not knowing if the funds would actually be available. Cambridge, on the other hand, offered the Indian American an open sesame for the research he wanted to pursue, which won him the shared Nobel today. C.V. Ramakrishnan told The Telegraph that he moved to the US in 1996, well after his retirement because Rajalakshmi had a stroke and their daughter, Lalita, now an assistant professor of microbiology and medicine at the University of Washington in Seattle, then a Stanford alumnus, wanted to be with her ailing mother. Since that first call at 2am today, the phones have not stopped ringing at the residences of Lalita Ramakrishnan and her father. Among the callers were India's consul-general in San Francisco, Susmita Gongulee Thomas, in whose charge Seattle falls. Unlike reporters, Venkatraman Ramakrishnan was considerate about his father's sleep and did not call until 5am although it was a cherished day for the entire family. |
| When, Venky? Nobel answers now Baroda friends recall how he wanted his research to help humanity | |||||||
| BASANT RAWAT | |||||||
Ahmedabad, Oct. 7: Venkatraman Ramakrishnan won the Nobel today, but for his old friends in Baroda, the honour had been long overdue. "Our Venky has got the Nobel prize!" exclaimed J.S. Bandukwala, a friend of the scientist. "It is a huge news, a great honour." Bandukwala, who taught physics at the Maharaj Sayajirao University of Baroda — of which the Nobel laureate is an alumnus — said it was only a matter of when, and not if, the award would come Venky's way. "For the last five years," Bandukwala said, "I have been hearing about his nomination for the coveted prize. I'm very happy. At last he has got the much-deserved recognition, which is indeed a great honour for the country." The winner of this year's chemistry prize — shared with two others — has his academic roots in the Gujarat city, where he grew up and did his graduation from. Ramakrishnan was born in the temple town of Chidambaram in Tamil Nadu in 1952. When he was two, his parents moved to Gujarat. Both his parents, father C.V. Ramakrishnan and mother Rajalakshmi, were scientists and taught biochemistry at the Maharaj Sayajirao University until they retired in the eighties. The elder Ramakrishnan, now 85, lives in Seattle, where daughter Lalita — also a scientist — teaches. Rajalakshmi, who did pioneering work on developing child nutrition in India, passed away two years ago.
It was natural that their children would follow in their footsteps. While "Venky" chose physics and later biochemistry, younger sister Lalita opted for medicine and is now a senior faculty member at the University of Washington in Seattle. After completing her MBBS from Baroda, Lalita did her PhD in immunology from Tufts University in Boston and followed it up with a post-doctoral from Stanford University. Although he got the Nobel for work on biochemistry, Ramakrishnan studied physics at the MS University of Baroda, graduating at the top of his class in 1971. Bandukwala remembers "Venky" not just as a scientist and a brilliant student, but as a multi-dimensional personality. "He is a music lover and an extremely kind-hearted secular person who cares for people," he said. "We are in regular touch over email and Venky has been very concerned about his old servant in Baroda. He has not forgotten his roots, though he has not visited Baroda for many years now." After his graduation, Ramakrishnan moved to the US for higher studies, and completed his PhD in physics from Ohio University in 1976. "Back in the seventies, the US was a natural destination for a budding scientist of his calibre," said Bandukwala. Old-timers in Baroda recalled that even while pursuing physics, Ramakrishnan was clear that he wanted to research on something that would help humanity. His monumental work on how the DNA code is translated into life has done just that, helping fight infectious disease and develop new antibiotics. Professor 'proud' Professor M.S. Govindarajan, who taught Venkatraman Ramakrishnan physics at Annamalai University, today said he was "extremely happy to hear that my student has won the Nobel prize for chemistry". "I am proud of him," Govindarajan told PTI. |
NOBEL PRIZE - CHEMISTRY
Mapping the ribosome at the atomic level
Venkatraman Ramakrishnan, MRC Laboratory, Cambridge.
The 2009 Nobel Prize in Chemistry is awarded for the detailed mapping of the ribosome – the cell's own protein factory. The ribosome translates the passive DNA information into form and function. The ribosome translates genetic information into action.
Ribosomes exist in all cells in all living organisms, from bacteria to human beings. As no living creature can survive without ribosomes, they are the perfect targets for drugs. Many of today's antibiotics attack the ribosomes of bacteria, but leave those of humans alone. The knowledge that this year's Nobel Laureates provide us with can thus be of substantial value for the development of new antibiotics. The three Nobel Prize Laureates in chemistry for 2009, Ada E. Yonath, Thomas A. Steitz and Venkatraman Ramakrishnan, are rewarded for mapping the ribosome – one of the cell's most complex machineries – at the atomic level. The ribosome reads the information in messenger RNA, and based upon that information, it produces protein. Scientists refer to this as translation.
The body contains tens of thousands of different proteins that control what happens in the body with an astounding precision.
The ribosomesA ribosome is about 25 nanometers (a millionth of a millimeter) in size. A cell contains tens of thousands of ribosomes. Scientists discovered that ribosomes are the locations where proteins are produced. In 1958 they named the protein-producing particle ribosome. It consists of proteins and RNA molecules (ribosomal RNA, or rRNA).
Thomas A. Steitz, Yale University, New Haven, U.S.
Scientists had identified DNA as the molecule that carries hereditary traits. The sequence of nucleotides controls the sequence of amino acids in proteins, which are produced by ribosomes in the cytoplasm. Yet, DNA and the ribosomes are located on different sides of the nuclear envelope and have no contact with one another.
The answer was provided at the beginning of the 1960s. Scientists realized that the genetic message is copied to a RNA molecule. They called it messenger RNA (mRNA). mRNA moves outside the nucleus and is caught by the ribosome, which uses mRNA as a blueprint for producing proteins.
A complex mechanism is involved by which information flows from DNA to RNA and become enzymes and other proteins. The image was still rather schematic, though. The way a molecule functions cannot be known unless the structure of the molecule is first known.
Hence it became very important to first produce the structure of ribosomes and understand how the atoms are located. It was only in 2000 that the structure that showed how the atoms are located in the ribosome was produced.
The ribosome reads the information in messenger RNA, and based upon that information, it produces protein. This picture is an X-ray crystallographic structure of 30S ribosomal particle from the `Thermus thermophilusâbacterium.
The pioneering and path-breaking effort was first started by Ada Yonath. At the end of the 1970s, she decided to try to generate X-ray crystallographic structures of the ribosome.
The prerequisite for X-ray crystallography is a perfect crystal of a molecule. To obtain high quality crystals from a protein can be a very tough task. And the larger the protein complex, the harder the task.
Exact locationThe ribosome is one of the most complicated protein/RNA complexes. It consists of hundreds of thousands of atoms. She wanted to establish the exact location of each and every one of these atoms in the ribosome. Many scientists thought this was very difficult task. And it was indeed one.
She studied the bacteria Geobacillus stearothermophilus can live in warm springs and survives in temperatures up to 75 degree C.
In 1980, she had already managed to generate the first three-dimensional crystals of the ribosome's large subunit. This was a great achievement, although the crystals were far from perfect. It would actually take another 20 years of hard work before she managed to generate an image of the ribosome where she could determine the location of each atom.
More scientists joined in the race when they realized that the ribosome's atomic structure could be mapped. Among them were Dr. Steitz and Dr. Ramakrishnan.
At the beginning of the 1990s, Dr. Yonath's crystals had sufficient quality. The pattern of black dots was detailed enough to determine the location of the atoms in the ribosome crystal. There remained a considerable obstacle, however. It was the "phase problem" of X-ray crystallography.
In order to determine a structure from the pattern of black dots (obtained during the process of X-ray crystallography), scientists needed to know the "phase angle" for each and every dot. This mathematical information is related to the location of the atoms in the crystal.
A trick frequently employed by scientists to determine phase angles is to soak the crystal in heavy atoms, e.g. mercury. The heavy atoms attach to the surface of the crystal's ribosomes. By comparing the dotted patterns from crystals with and without heavy atoms, scientists can establish the phase angle
However, as the ribosomes are so large, too many heavy atoms attached to the ribosome, and it was difficult to immediately determine the phase angle. Additional information was therefore needed in order to solve the phase problem.
It was Dr. Steitz who finally solved the problem. He used images of the ribosome, generated by Joachim Frank, a specialist in electron microscopy. With the help of those images, Dr. Steitz could find out how the ribosomes were oriented and located within the crystal (but the resolution did not allow him to see individual atoms). This information, together with the information from the heavy atoms, finally yielded the phase angle.
In 1998, Dr. Steitz published the first crystal structure of the ribosome's large subunit. But it was not possible to see individual atoms, but one could detect the ribosome's long RNA molecules. This was a decisive breakthrough.
Now that the phase problem had finally been solved, all that remained was to improve the crystals and collect more data, in order to increase the sharpness of the image.
In August and September 2000, they published crystal structures with resolutions that allowed interpretation of the atomic locations. Dr. Steitz managed to obtain the structure of the large subunit from Haloarcula marismortui. Dr. Yonath and Dr. Ramakrishnan obtained the structure of the small subunit from Thermus thermophilus. Thus it was possible to map ribosome functionality at the most basic, atomic level.
Molecular rulerA property of the ribosome, that has fascinated scientists for a long time, is that it seldom makes any errors when it translates DNA/RNA-language into protein language.
If an amino acid is incorrectly incorporated, the protein can entirely lose its function, or perhaps even worse, begin to function differently. For the correct amino acid to be selected depends primarily on the base pairs formed between tRNA and mRNA.
However, this pairing process is not sufficient to explain the ribosome's precision. Dr. Ramakrishnan's crystal structures of the ribosome's small subunit have been crucial for the understanding of how the ribosome achieves its precision. He identified something that could be described as a molecular ruler.
Nucleotides in the small sub-unit's rRNA measure the distance between the codon in mRNA and the anticodon in tRNA. If the distance is incorrect, the tRNA molecule falls off the ribosome. Using the ruler twice, the ribosome double-checks that everything is correct. This ensures that errors only occur about once per 1,00,000 amino acids.
Search for antibioticsThe Laureates' work proves useful in the search for new antibiotics.
The ribosome is the target for new antibiotics. Today, humans have an arsenal of different antibiotics which can be used in the fight against disease-generating bacteria. Many of these antibiotics kill bacteria by blocking the functions of their ribosomes.
However, bacteria have become resistant to most of these drugs at an ominous rate. Therefore we need new ones. This year's three Nobel Laureates in chemistry have all produced structures that show how different antibiotics bind to the ribosome.
Some of them block the tunnel through which the growing proteins leave the ribosome, others prevent the formation of the peptide bond between amino acids. Still others corrupt the translation from DNA/RNA-language into protein language.
Several companies now use the structures of the ribosome in order to develop new antibiotics. Some of these are currently undergoing clinical tests, in order to come to grips with the problem of multiresistant bacteria (e.g. MRSA).
The understanding of the ribosome's structure and function is of great and immediate use to humanity. The discoveries that the three have made, are important both for the understanding of how life's core processes function, and in order to save lives.
(Edited excerpts from public information available at www.nobelprize.org)
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Common root: Tamil Nadu gets its third laureate
| Subramanyan Chandrasekhar, who won the Nobel Prize for physics in 1983, had a family link to the country's first Nobel laureate, Sir C V Raman, who
However, all three winners of the Nobel in sciences have a connect beyond names. Their roots are in Tamil Nadu and they share a family background conducive to intellectual and scientific pursuits. Raman's father, Chandrasekhara Iyer was a school teacher and a lecturer in mathematics and physics. Chandrasekhar's father, C S Iyer, was a musician and musicologist. Ramakrishnan's parents were scientists. Twentieth century Tamil Nadu, thus, has the distinction of producing three Nobel laureates in science, although only the earliest — Raman — was awarded for his work in India. And it is a tradition that includes the mathematical genius Srinivasan Ramanujan who died too young to achieve wider fame within his lifetime. Raman was born in 1888 in Tiruchi and graduated from Presidency College in Chennai. Chandrasekhar also went to Presidency College after Hindu High School, Triplicane, though he was born in Lahore. Ramakrishnan, born in Chidambaram, the temple town in northern Tamil Nadu, graduated from Baroda University in physics, and shifted to biology while pursuing higher studies in the United States. Raman's prize in 1930 was for his work on the scattering of light in liquids and for the discovery of the 'Raman Effect' — which confirmed that light is made up of 'photons', or elementary particles that form the basic unit of light. The Raman Effect is considered an important tool in analysing the composition of solids, liquids and gases. At around the same time, Chandra, the Indo—American astrophysicist, was computing the mass of a star beyond which it will collapse to become a neutron star or a black hole. It was for this early work on the physical processes relating to the evolution of stars that he was given the Nobel in 1983. | ||
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