Venki Ramakrishnan

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Ramakrishnan is internationally recognised for determination of the atomic structure of the 30S ribosomal subunit. Earlier he mapped the arrangement of proteins in the 30S subunit by neutron diffraction and solved X-ray structures of individual components and their RNA complexes. Fundamental insights came from his crystallographic studies of the complete 30S subunit. The atomic model included over 1500 bases of RNA and 20 associated proteins. The RNA interactions representing the P-site tRNA and the mRNA binding site were identified and the likely modes of action of many clinically important antibiotics determined. His most recent work goes to the heart of the decoding mechanism showing the 30S subunit complexed with poly-U mRNA and the stem-loop of the cognate phenylalanine tRNA. Anti-codon recognition leaves the "wobble" base free to accommodate certain non-Watson/Crick basepairs, thus providing an atomic description of both codon:anti-codon recognition and "wobble". He has also made substantial contributions to understanding how chromatin is organised, particularly the structure of linker histones and their role in higher order folding. [53]

In 2020, he was elected to the American Philosophical Society [54] and became a board member of The British Library. [55]

Ramakrishnan was made a Member of the Order of Merit (OM) in 2022. [5]

Personal life

In 1975, Ramakrishnan married Vera Rosenberry, an author and illustrator of children's books. [1] He has a step-daughter, Tanya Kapka, a physician specializing in public health and health-care delivery to under-served communities; and a son, Raman Ramakrishnan, a cellist specializing in chamber music and professor at Bard College. [56]

Selected publications

Related Research Articles

<span class="mw-page-title-main">Ribosome</span> Synthesizes proteins in cells

Ribosomes are macromolecular machines, found within all cells, that perform biological protein synthesis. Ribosomes link amino acids together in the order specified by the codons of messenger RNA molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA molecules and many ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.

<span class="mw-page-title-main">Translation (biology)</span> Cellular process of protein synthesis

In biology, translation is the process in living cells in which proteins are produced using RNA molecules as templates. The generated protein is a sequence of amino acids. This sequence is determined by the sequence of nucleotides in the RNA. The nucleotides are considered three at a time. Each such triple results in addition of one specific amino acid to the protein being generated. The matching from nucleotide triple to amino acid is called the genetic code. The translation is performed by a large complex of functional RNA and proteins called ribosomes. The entire process is called gene expression.

<span class="mw-page-title-main">Ribosomal RNA</span> RNA component of the ribosome, essential for protein synthesis in all living organisms

Ribosomal ribonucleic acid (rRNA) is a type of non-coding RNA which is the primary component of ribosomes, essential to all cells. rRNA is a ribozyme which carries out protein synthesis in ribosomes. Ribosomal RNA is transcribed from ribosomal DNA (rDNA) and then bound to ribosomal proteins to form small and large ribosome subunits. rRNA is the physical and mechanical factor of the ribosome that forces transfer RNA (tRNA) and messenger RNA (mRNA) to process and translate the latter into proteins. Ribosomal RNA is the predominant form of RNA found in most cells; it makes up about 80% of cellular RNA despite never being translated into proteins itself. Ribosomes are composed of approximately 60% rRNA and 40% ribosomal proteins, though this ratio differs between prokaryotes and eukaryotes.

Bacterial translation is the process by which messenger RNA is translated into proteins in bacteria.

<span class="mw-page-title-main">MRC Laboratory of Molecular Biology</span> Research institute in Cambridge, England

The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health.

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A ribosomal protein is any of the proteins that, in conjunction with rRNA, make up the ribosomal subunits involved in the cellular process of translation. E. coli, other bacteria and Archaea have a 30S small subunit and a 50S large subunit, whereas humans and yeasts have a 40S small subunit and a 60S large subunit. Equivalent subunits are frequently numbered differently between bacteria, Archaea, yeasts and humans.

Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Several initiation factors form a complex with the small 40S ribosomal subunit and Met-tRNAiMet called the 43S preinitiation complex. Additional factors of the eIF4F complex recruit the 43S PIC to the five-prime cap structure of the mRNA, from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNAiMet promotes gated phosphate and eIF1 release to form the 48S preinitiation complex, followed by large 60S ribosomal subunit recruitment to form the 80S ribosome. There exist many more eukaryotic initiation factors than prokaryotic initiation factors, reflecting the greater biological complexity of eukaryotic translation. There are at least twelve eukaryotic initiation factors, composed of many more polypeptides, and these are described below.

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<span class="mw-page-title-main">5S ribosomal RNA</span> RNA component of the large subunit of the ribosome

The 5S ribosomal RNA is an approximately 120 nucleotide-long ribosomal RNA molecule with a mass of 40 kDa. It is a structural and functional component of the large subunit of the ribosome in all domains of life, with the exception of mitochondrial ribosomes of fungi and animals. The designation 5S refers to the molecule's sedimentation velocity in an ultracentrifuge, which is measured in Svedberg units (S).

<span class="mw-page-title-main">Prokaryotic large ribosomal subunit</span>

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<span class="mw-page-title-main">Prokaryotic small ribosomal subunit</span> Smaller subunit of the 70S ribosome found in prokaryote cells

The prokaryotic small ribosomal subunit, or 30S subunit, is the smaller subunit of the 70S ribosome found in prokaryotes. It is a complex of the 16S ribosomal RNA (rRNA) and 19 proteins. This complex is implicated in the binding of transfer RNA to messenger RNA (mRNA). The small subunit is responsible for the binding and the reading of the mRNA during translation. The small subunit, both the rRNA and its proteins, complexes with the large 50S subunit to form the 70S prokaryotic ribosome in prokaryotic cells. This 70S ribosome is then used to translate mRNA into proteins.

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<span class="mw-page-title-main">EF-G</span> Prokaryotic elongation factor

EF-G is a prokaryotic elongation factor involved in mRNA translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.

The eukaryotic small ribosomal subunit (40S) is the smaller subunit of the eukaryotic 80S ribosomes, with the other major component being the large ribosomal subunit (60S). The "40S" and "60S" names originate from the convention that ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. It is structurally and functionally related to the 30S subunit of 70S prokaryotic ribosomes. However, the 40S subunit is much larger than the prokaryotic 30S subunit and contains many additional protein segments, as well as rRNA expansion segments.

<span class="mw-page-title-main">Eukaryotic ribosome</span> Large and complex molecular machine

Ribosomes are a large and complex molecular machine that catalyzes the synthesis of proteins, referred to as translation. The ribosome selects aminoacylated transfer RNAs (tRNAs) based on the sequence of a protein-encoding messenger RNA (mRNA) and covalently links the amino acids into a polypeptide chain. Ribosomes from all organisms share a highly conserved catalytic center. However, the ribosomes of eukaryotes are much larger than prokaryotic ribosomes and subject to more complex regulation and biogenesis pathways. Eukaryotic ribosomes are also known as 80S ribosomes, referring to their sedimentation coefficients in Svedberg units, because they sediment faster than the prokaryotic (70S) ribosomes. Eukaryotic ribosomes have two unequal subunits, designated small subunit (40S) and large subunit (60S) according to their sedimentation coefficients. Both subunits contain dozens of ribosomal proteins arranged on a scaffold composed of ribosomal RNA (rRNA). The small subunit monitors the complementarity between tRNA anticodon and mRNA, while the large subunit catalyzes peptide bond formation.

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<span class="mw-page-title-main">Translation initiation factor IF-3</span>

In molecular biology, translation initiation factor IF-3 is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consists of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA. IF-3 is a basic protein that binds to the 30S ribosomal subunit. The chloroplast homolog enhances the poly(A,U,G)-dependent binding of the initiator tRNA to its ribosomal 30s subunits. IF1–IF3 may also perform ribosome recycling.

<span class="mw-page-title-main">Ada Yonath</span> Israeli chemist (born 1939)

Ada E. Yonath is an Israeli crystallographer and Nobel laureate in Chemistry, best known for her pioneering work on the structure of ribosomes. She is the current director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly of the Weizmann Institute of Science.

<span class="mw-page-title-main">50S ribosomal protein L25</span>

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<span class="mw-page-title-main">Andrew P. Carter</span> British structural biologist

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References

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  7. 1 2 Ramakrishnan, Venkatraman; Tanaka, Tomoyasu (1977). "Green's-function theory of the ferroelectric phase transition in potassium dihydrogen phosphate (KDP)". Physical Review B . 16 (1): 422–426. Bibcode:1977PhRvB..16..422R. doi:10.1103/physrevb.16.422.
  8. 1 2 Cerf, Corinne; Lippens, Guy; Muyldermans, Serge; Segers, Alain; Ramakrishnan, V.; Wodak, Shoshana J.; Hallenga, Klaas; Wyns, Lode (1993). "Homo- and heteronuclear two-dimensional NMR". Biochemistry. 32 (42): 11345–11351. doi:10.1021/bi00093a011. PMID   8218199.
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  16. ↑ Ramakrishnan, Venki (2018). Gene machine. The race to decipher the secrets of the ribosome. London: Oneworld. ISBN   9781786074362. OCLC   1080631601.
  17. ↑ Peplow, M. (2015). "Structural biologist named president of UK Royal Society". Nature. doi: 10.1038/nature.2015.17153 . S2CID   112623895.
  18. ↑ "Common root: Tamil Nadu gets its third laureate". Times of India. TNN. 8 October 2009.
  19. ↑ "Venki Ramakrishnan, Ph.D." American Academy of Achievement. Retrieved 26 November 2022.
  20. ↑ Ramakrishnan, C. V.; Banerjee, B. N. (1951). "Mould Lipase: Effect of Addition of Vitamins and Sterol to the Cake Medium on the Growth and the Activity of the Lipolytic Mould". Nature. 168 (4282): 917–918. Bibcode:1951Natur.168..917R. doi:10.1038/168917a0. PMID   14899529. S2CID   4244697.
  21. ↑ Ramakrishnan, Rajalakshmi (1959). Comparative Effects of Successive and Simultaneous Presentation on Transfer in Verbal Learning (PhD thesis). McGill University. ProQuest   301865011.
  22. ↑ "Lalita Ramakrishnan Home page in Department of Medicine, University of Cambridge".
  23. ↑ "Lalita Ramakrishnan elected to the U.S. National Academy of Sciences". University of Cambridge. Retrieved 30 January 2016.
  24. ↑ Ramakrishnan, Venkatraman (1976). The Green function theory of the ferroelectric phase transition in KDP (PhD thesis). Ohio University. OCLC   3079828. ProQuest   302809453.
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  26. ↑ "Factbox: Nobel chemistry prize – Who are the winners?". Reuters. 7 October 2009. Retrieved 7 October 2009.
  27. ↑ "Profile: Dr Venkatraman Ramakrishnan". Indian Express . 7 October 2009. Retrieved 7 October 2009.
  28. ↑ "Nobel laureate Venkat Ramakrishnan failed IIT, medical entrance tests". The Times of India. 5 January 2010.
  29. ↑ "Venki Ramakrishnan, Ph.D. Biography and Interview". www.achievement.org. American Academy of Achievement . Retrieved 30 December 2022.
  30. ↑ Fernández, Israel S.; Bai, Xiao-Chen; Hussain, Tanweer; Kelley, Ann C.; Lorsch, Jon R.; Ramakrishnan, V.; Scheres, Sjors H. W. (15 November 2013). "Molecular architecture of a eukaryotic translational initiation complex". Science. 342 (6160): 1240585. doi:10.1126/science.1240585. ISSN   1095-9203. PMC   3836175 . PMID   24200810.
  31. ↑ Amunts, Alexey; Brown, Alan; Bai, Xiao-Chen; Llácer, Jose L.; Hussain, Tanweer; Emsley, Paul; Long, Fei; Murshudov, Garib; Scheres, Sjors H. W. (28 March 2014). "Structure of the yeast mitochondrial large ribosomal subunit". Science. 343 (6178): 1485–1489. Bibcode:2014Sci...343.1485A. doi:10.1126/science.1249410. ISSN   1095-9203. PMC   4046073 . PMID   24675956.
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  34. ↑ Ramakrishnan, V.; Carter, Andrew P.; Clemons, William M.; Brodersen, Ditlev E.; Morgan-Warren, Robert J.; Wimberly, Brian T. (2000). "Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics". Nature . 407 (6802): 340–348. Bibcode:2000Natur.407..340C. doi:10.1038/35030019. PMID   11014183. S2CID   4408938.
  35. ↑ Ramakrishnan, V.; Finch, J. T.; Graziano, V.; Lee, P. L.; Sweet, R. M. (1993). "Crystal structure of globular domain of histone H5 and its implications for nucleosome binding". Nature . 362 (6417): 219–223. Bibcode:1993Natur.362..219R. doi:10.1038/362219a0. PMID   8384699. S2CID   4301198.
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Venki Ramakrishnan
Venki Ramakrishnan (cropped).jpg
Ramakrishnan in 2015
62nd President of the Royal Society
In office
1 December 2015 –30 November 2020
Spouse
Vera Rosenberry
​
(m. 1975)​
[1]
Children1 [1]
Parent
Relatives Lalita Ramakrishnan (sister)
ResidenceUnited Kingdom
Website www2.mrc-lmb.cam.ac.uk/group-leaders/n-to-s/venki-ramakrishnan
Known for
Awards
Academic background
Education
Alma mater Ohio University
Thesis The Green Function Theory of the Ferroelectric Phase Transition in Potassium Dihydrogen-Phosphate  (1976)
Doctoral advisorTomoyasu Tanaka [1] [7]
Professional and academic associations
Preceded by62nd President of the Royal Society
2015–2020		Succeeded by
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