Venkatraman "Venki" Ramakrishnan (born 1952)[2] is an American and British structural biologist of Indian origin. He was elected President of the Royal Society in November 2015; Presidents serve for five years.[8] In 2009 he shared the Nobel Prize in Chemistry with Thomas A. Steitz and Ada Yonath, "for studies of the structure and function of the ribosome".[3][9][10][11][12]
Since 1999, he has worked as a group leader at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) on the Cambridge Biomedical Campus, UK.[13][14]
Ramakrishnan was born in Chidambaram in Cuddalore district of Tamil Nadu, India[15] to C. V. Ramakrishnan and Rajalakshmi Ramakrishnan in a Tamil Iyer family. Both his parents were scientists, and his father was head of the Department of Biochemistry at the Maharaja Sayajirao University of Baroda.[1][16][17] At the time of his birth, Ramakrishnan's father was away from India doing postdoctoral research with David E. Green at the University of Wisconsin–Madison in the US.[1]
His mother obtained a PhD in Psychology from McGill University in 1959[18] which she completed in only 18 months, and was mentored by Donald O. Hebb.[1] Lalita Ramakrishnan, his younger sister, is professor of immunology and infectious diseases at the Department of Medicine, University of Cambridge,[19] and is a member of the National Academy of Sciences.[20]
Ramakrishnan moved to Vadodara (previously also known as Baroda) in Gujarat at the age of three, where he had his schooling at Convent of Jesus and Mary, except for spending 1960–61 in Adelaide, Australia. Following his pre-science at the Maharaja Sayajirao University of Baroda, he did his undergraduate studies in the same university on a National Science Talent Scholarship, graduating with a Bachelor of Science degree in Physics in 1971.[10] At the time, the physics course at Baroda was new, and based in part on The Berkeley Physics Course and The Feynman Lectures on Physics.[1]
Ramakrishnan began work on ribosomes as a postdoctoral fellow with Peter Moore at Yale University.[10] After his post-doctoral fellowship, he initially could not find a faculty position even though he had applied to about 50 universities in the U.S.[25]
He continued to work on ribosomes from 1983-95 as a staff scientist at Brookhaven National Laboratory.[6] In 1995 he moved to the University of Utah as a Professor of Biochemistry, and in 1999, he moved to his current position at the Medical Research Council Laboratory of Molecular Biology in Cambridge, England, where he had also been a sabbatical visitor during 1991-92.
In 1999, Ramakrishnan's laboratory published a 5.5 Angstrom resolution structure of the 30S subunit. The following year, his laboratory determined the complete molecular structure of the 30S subunit of the ribosome and its complexes with several antibiotics. This was followed by studies that provided structural insights into the mechanism that ensures the fidelity of protein biosynthesis. In 2007, his laboratory determined the atomic structure of the whole ribosome in complex with its tRNA and mRNA ligands. Since 2013, he has primarily used cryo-EM to determine new ribosome structures.[26][27] Ramakrishnan is also known for his past work on histone and chromatin structure.
In an interview in July 2018, he said that Britain's decision to leave the European Union (Brexit) was hurting Britain's reputation as a good place to work in science, commenting "It’s very hard for the science community to see any advantages in Brexit. They are pretty blunt about that." He saw advantages to both the UK and the EU for Britain to continue to be engaged in Galileo and Euratom, which, unlike the European Medicines Agency, are not EU agencies.[37]
Awards and honours
Ramakrishnan at the Nobel Prize Press conference in 2009.
Knight Bachelor's badge, to which Ramakrishnan became entited in the 2012 New Year Honours
Ramakrishnan was elected a Member of the European Molecular Biology Organization (EMBO) in 2002,[38] a Fellow of the Royal Society (FRS) in 2003,[39] and a Member of the U.S. National Academy of Sciences in 2004. In 2007, Ramakrishnan was awarded the Louis-Jeantet Prize for Medicine and the Datta Lectureship and Medal of the Federation of European Biochemical Societies (FEBS). In 2008, he won the Heatley Medal of the British Biochemical Society. Since 2008, he is a Fellow of Trinity College, Cambridge and a foreign Fellow of the Indian National Science Academy. He was elected an Honorary Fellow of the Academy of Medical Sciences in 2010, and has received honorary degrees from the Maharaja Sayajirao University of Baroda, University of Utah and University of Cambridge. He is also an Honorary Fellow of Somerville College, Oxford.[40]
In 2009, Ramakrishnan was awarded the Nobel Prize in Chemistry along with Thomas A. Steitz and Ada Yonath.[41] He received India's second highest civilian honor, the Padma Vibhushan, in 2010.[42] Ramakrishnan was knighted in the 2012 New Year Honours for services to Molecular Biology,[5] but does not generally use the title 'Sir'.[43] In the same year, he was awarded the Sir Hans Krebs Medal by the FEBS. In 2014, he was awarded the XLVI Jiménez-Díaz Prize by the Fundación Conchita Rábago (Spain). Ramakrishnan was included as one of 25 Greatest Global Living Indians by NDTV Channel, India on 14 December 2013. His certificate of election to the Royal Society reads:
“
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-sitetRNA 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.[44]
”
Views
Ramakrishnan fears a no deal Brexit would harm science. Ramakrishnan wrote, "A deal on science is in the best interests of Europe as a whole and should not be sacrificed as collateral damage over disagreements on other issues. If we are going to successfully tackle global problems like climate change, human disease and food security, we can’t do so in isolation. There is no scenario where trashing our relationships with our closest scientific collaborators in the EU gets us closer to these goals."[45]
Personal life
Ramakrishnan married Vera Rosenberry, an author and illustrator of children's books, in 1975.[1] His stepdaughter Tanya Kapka is a doctor in Oregon, and his son Raman Ramakrishnan is a cellist based in New York.[46]
↑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". Nature168 (4282): 917–918. doi:10.1038/168917a0. PMID14899529.
↑Ramakrishnan, V.; Wimberly, Brian T.; Brodersen, Ditlev E.; Clemons, William M.; Morgan-Warren, Robert J.; Carter, Andrew P.; Vonrhein, Clemens; Hartsch, Thomas (2000). "Structure of the 30S ribosomal subunit". Nature407 (6802): 327–339. doi:10.1038/35030006. PMID11014182.
↑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". Nature407 (6802): 340–348. doi:10.1038/35030019. PMID11014183.
↑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". Nature362 (6417): 219–223. doi:10.1038/362219a0. PMID8384699.
↑Ogle, J. M.; Brodersen, DE; Clemons, WM Jr; Tarry, MJ; Carter, AP; Ramakrishnan, V (2001). "Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit". Science292 (5518): 897–902. doi:10.1126/science.1060612. PMID11340196.
↑Semenza, C; Butterworth, B; Panzeri, M; Ferreri, T (1990). "Word formation: New evidence from aphasia". Neuropsychologia28 (5): 499–502. doi:10.1016/0028-3932(90)90075-y. PMID1695997.
↑Brodersen, Ditlev E.; Clemons, William M.; Carter, Andrew P.; Morgan-Warren, Robert J.; Wimberly, Brian T.; Ramakrishnan, V. (2000). "The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit". Cell103 (7): 1143–1154. doi:10.1016/s0092-8674(00)00216-6. PMID11163189.
↑Ogle, James M.; Murphy, Frank V.; Tarry, Michael J.; Ramakrishnan, V. (2002). "Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form". Cell111 (5): 721–732. doi:10.1016/s0092-8674(02)01086-3. PMID12464183.