Ramakrishnan in 2015
|62ndPresident of the Royal Society|
|Preceded by||Paul Nurse|
1952 (age 66–67)
Chidambaram, Tamilnadu, India
Vera Rosenberry(m. 1975)
|Children||1 son, 1 stepdaughter|
|Thesis||The Green Function Theory of the Ferroelectric Phase Transition in Potassium Dihydrogen-Phosphate (1976)|
|Doctoral advisor||Tomoyasu Tanaka|
|Doctoral students||Nathan James|
|Wikimedia Commons has media related to Geobiography of Venkatraman Ramakrishnan .|
Venkatraman "Venki" Ramakrishnan (born 1952)is an American and British structural biologist of Indian origin. 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". . He was elected President of the Royal Society for a term of five years starting in 2015. .
Structural biology is a branch of molecular biology, biochemistry, and biophysics concerned with the molecular structure of biological macromolecules, how they acquire the structures they have, and how alterations in their structures affect their function. This subject is of great interest to biologists because macromolecules carry out most of the functions of cells, and it is only by coiling into specific three-dimensional shapes that they are able to perform these functions. This architecture, the "tertiary structure" of molecules, depends in a complicated way on each molecule's basic composition, or "primary structure."
The Nobel Prize in Chemistry is awarded annually by the Royal Swedish Academy of Sciences to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel in 1895, awarded for outstanding contributions in chemistry, physics, literature, peace, and physiology or medicine. This award is administered by the Nobel Foundation, and awarded by Royal Swedish Academy of Sciences on proposal of the Nobel Committee for Chemistry which consists of five members elected by Academy. The award is presented in Stockholm at an annual ceremony on December 10, the anniversary of Nobel's death.
Thomas Arthur Steitz was an American biochemist, a Sterling Professor of Molecular Biophysics and Biochemistry at Yale University, and investigator at the Howard Hughes Medical Institute, best known for his pioneering work on the ribosome.
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.
The Medical Research Council (MRC) is responsible for co-coordinating and funding medical research in the United Kingdom. It is part of United Kingdom Research and Innovation (UKRI), which came into operation 1 April 2018, and brings together the UK’s seven research councils, Innovate UK and Research England. UK Research and Innovation is answerable to, although politically independent from, the Department for Business, Energy and Industrial Strategy.
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 with a much broader focus. A new £212m replacement building constructed close by to the original site on the Cambridge Biomedical Campus was opened in May 2013. The road outside the new building is named Francis Crick Avenue after the 1962 joint Nobel Prize winner, who co-discovered the helical structure of DNA in 1953.
The Cambridge Biomedical Campus is the largest centre of medical research and health science in Europe. Located at the southern end of Hills Road in Cambridge, England the campus is managed by the University of Cambridge. The site is funded by organisations such as the Cambridge University Hospitals NHS Foundation Trust, the Wellcome Trust, Cancer Research UK, the UK government's Medical Research Council and has National Institute for Health Research Biomedical Research Centre status. It is an accredited UK academic health science centre and home to Addenbrooke's Hospital and the university's medical school.
Ramakrishnan was born in Chidambaram in Cuddalore district of Tamil Nadu, Indiato C. V. Ramakrishnan and Rajalakshmi Ramakrishnan. Both his parents were scientists, and his father was head of the Department of Biochemistry at the Maharaja Sayajirao University of Baroda. 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.
Chidambaram is a town and municipality in Cuddalore district in the Indian state of Tamil Nadu. It is the headquarters of the Chidambaram taluk. The town is believed to be of significant antiquity and has been ruled, at different times, by the Pallavas until 9th century, Medieval Cholas, Later Cholas, Later Pandyas, Vijayanagar Empire, Marathas and the British. The town is known for the Thillai Nataraja Temple, and the annual chariot festival held in the months of December–January and June to July
Cuddalore District is one of the districts of the south Indian state of Tamil Nadu. The city of Cuddalore is the district headquarters. According to the 2011 Census, Cuddalore district had a population of 2,605,914 with a sex-ratio of 987 females for every 1,000 males.
Tamil Nadu is one of the 29 states of India. Its capital and largest city is Chennai. Tamil Nadu lies in the southernmost part of the Indian subcontinent and is bordered by the union territory of Puducherry and the South Indian states of Kerala, Karnataka, and Andhra Pradesh. It is bounded by the Eastern Ghats on the north, by the Nilgiri Mountains, the Meghamalai Hills, and Kerala on the west, by the Bay of Bengal in the east, by the Gulf of Mannar and the Palk Strait on the southeast, and by the Indian Ocean on the south. The state shares a maritime border with the nation of Sri Lanka.
His mother obtained a PhD in Psychology from McGill University in 1959which she completed in only 18 months, and was mentored by Donald O. Hebb. Lalita Ramakrishnan, his younger sister, is professor of immunology and infectious diseases at the Department of Medicine, University of Cambridge, and is a member of the National Academy of Sciences.
Psychology is the science of behavior and mind. Psychology includes the study of conscious and unconscious phenomena, as well as feeling and thought. It is an academic discipline of immense scope. Psychologists seek an understanding of the emergent properties of brains, and all the variety of phenomena linked to those emergent properties. As a social science it aims to understand individuals and groups by establishing general principles and researching specific cases.
McGill University is a public research university in Montreal, Quebec, Canada. It was established in 1821 by royal charter, granted by King George IV. The university bears the name of James McGill, a Montreal merchant originally from Scotland whose bequest in 1813 formed the university's precursor, McGill College.
Donald Olding Hebb FRS was a Canadian psychologist who was influential in the area of neuropsychology, where he sought to understand how the function of neurons contributed to psychological processes such as learning. He is best known for his theory of Hebbian learning, which he introduced in his classic 1949 work The Organization of Behavior. He has been described as the father of neuropsychology and neural networks. A Review of General Psychology survey, published in 2002, ranked Hebb as the 19th most cited psychologist of the 20th century. His views on learning described behavior and thought in terms of brain function, explaining cognitive processes in terms of connections between neuron assemblies.
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.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.
Vadodara is the third-largest city in the Indian state of Gujarat, after Ahmedabad and Surat. It is the administrative headquarters of Vadodara District and is located on the banks of the Vishwamitri river, 141 kilometres (88 mi) from the state capital Gandhinagar. The railway line and NH 8 that connect Delhi and Mumbai pass through Vadodara. It is known as a Sanskari city of India.
Gujarat is a state on the western coast of India with a coastline of 1,600 km (990 mi) – most of which lies on the Kathiawar peninsula – and a population in excess of 60 million. It is the sixth largest Indian state by area and the ninth largest state by population. Gujarat is bordered by Rajasthan to the northeast, Daman and Diu to the south, Dadra and Nagar Haveli and Maharashtra to the southeast, Madhya Pradesh to the east, and the Arabian Sea and the Pakistani province of Sindh to the west. Its capital city is Gandhinagar, while its largest city is Ahmedabad. The Gujarati-speaking people of India are indigenous to the state. The economy of Gujarat is the third-largest state economy in India with ₹14.96 lakh crore (US$210 billion) in gross domestic product and a per capita GDP of ₹157,000 (US$2,200).
Adelaide is the capital city of the state of South Australia, and the fifth-most populous city of Australia. In June 2017, Adelaide had an estimated resident population of 1,333,927. Adelaide is home to more than 75 percent of the South Australian population, making it the most centralised population of any state in Australia.
Immediately after graduation he moved to the U.S., where he obtained his Doctor of Philosophy degree in Physics from Ohio University in 1976 for research into the ferroelectric phase transition of potassium dihydrogen phosphate (KDP)supervised by Tomoyasu Tanaka. He then spent two years studying biology as a graduate student at the University of California, San Diego while making a transition from theoretical physics to biology.
A Doctor of Philosophy is the highest university degree that is conferred after a course of study by universities in most English-speaking countries. PhDs are awarded for programs across the whole breadth of academic fields. As an earned research degree, those studying for a PhD are usually required to produce original research that expands the boundaries of knowledge, normally in the form of a thesis or dissertation, and defend their work against experts in the field. The completion of a PhD is often a requirement for employment as a university professor, researcher, or scientist in many fields. Individuals who have earned a Doctor of Philosophy degree may, in many jurisdictions, use the title Doctor or, in non-English-speaking countries, variants such as "Dr. phil." with their name, although the proper etiquette associated with this usage may also be subject to the professional ethics of their own scholarly field, culture, or society. Those who teach at universities or work in academic, educational, or research fields are usually addressed by this title "professionally and socially in a salutation or conversation." Alternatively, holders may use post-nominal letters such as "Ph.D.", "PhD", or "DPhil". It is, however, considered incorrect to use both the title and post-nominals at the same time.
Ohio University is a public research university in Athens, Ohio. The first university chartered by an Act of Congress and the first to be chartered in Ohio, it was chartered in 1787 by the Congress of the Confederation and subsequently approved for the territory in 1802 and state in 1804, opening for students in 1809. Ohio University is the oldest university in Ohio, the eighth oldest public university in the United States and the 30th oldest university among public's and privates. As of fall 2018, the university's total enrollment at Athens was 20,000, while the all- campus enrollment was just under 35,000.
Ferroelectricity is a characteristic of certain materials that have a spontaneous electric polarization that can be reversed by the application of an external electric field. All ferroelectrics are pyroelectric, with the additional property that their natural electrical polarization is reversible. The term is used in analogy to ferromagnetism, in which a material exhibits a permanent magnetic moment. Ferromagnetism was already known when ferroelectricity was discovered in 1920 in Rochelle salt by Valasek. Thus, the prefix ferro, meaning iron, was used to describe the property despite the fact that most ferroelectric materials do not contain iron. Materials that are both ferroelectric and ferromagnetic are known as multiferroics.
Ramakrishnan began work on ribosomes as a postdoctoral fellow with Peter Moore at Yale University.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.
He continued to work on ribosomes from 1983-95 as a staff scientist at Brookhaven National Laboratory.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 on a Guggenheim Fellowship.
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.Ramakrishnan is also known for his past work on histone and chromatin structure.
As of 2015 [update] his most cited papers (according to Scopus ) have been published in Nature , Science , and Cell .
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.
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."
Ramakrishnan was elected a Member of the European Molecular Biology Organization (EMBO) in 2002,a Fellow of the Royal Society (FRS) in 2003, 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.
In 2009, Ramakrishnan was awarded the Nobel Prize in Chemistry along with Thomas A. Steitz and Ada Yonath.He received India's second highest civilian honor, the Padma Vibhushan, in 2010. Ramakrishnan was knighted in the 2012 New Year Honours for services to Molecular Biology, but does not generally use the title 'Sir'. 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-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.
Ramakrishnan married Vera Rosenberry, an author and illustrator of children's books, in 1975.His stepdaughter Tanya Kapka is a doctor in Oregon, and his son Raman Ramakrishnan is a cellist based in New York.
Ribonucleic acid (RNA) is a polymeric molecule essential in various biological roles in coding, decoding, regulation and expression of genes. RNA and DNA are nucleic acids, and, along with lipids, proteins and carbohydrates, constitute the four major macromolecules essential for all known forms of life. Like DNA, RNA is assembled as a chain of nucleotides, but unlike DNA it is more often found in nature as a single-strand folded onto itself, rather than a paired double-strand. Cellular organisms use messenger RNA (mRNA) to convey genetic information that directs synthesis of specific proteins. Many viruses encode their genetic information using an RNA genome.
The ribosome is a complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis (translation). Ribosomes link amino acids together in the order specified by messenger RNA (mRNA) molecules. Ribosomes consist of two major components: the small ribosomal subunits, which read the RNA, and the large subunits, which join amino acids to form a polypeptide chain. Each subunit consists of one or more ribosomal RNA (rRNA) molecules and a variety of ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.
Ribosomal ribonucleic acid (rRNA) is the RNA component of the ribosome, and is essential for protein synthesis in all living organisms. It constitutes the predominant material within the ribosome, which is approximately 60% rRNA and 40% protein by weight, or 3/5 of ribosome mass. Ribosomes contain two major rRNAs and 50 or more proteins. The ribosomal RNAs form two subunits, the large subunit (LSU) and small subunit (SSU). The LSU rRNA acts as a ribozyme, catalyzing peptide bond formation. The SSU and LSU rRNA sequences are widely used for working out evolutionary relationships among organisms, since they are of ancient origin and are found in all known forms of life.
Prokaryotic translation is the process by which messenger RNA is translated into proteins in prokaryotes.
Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recycling.
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. A large part of the knowledge about these organic molecules has come from the study of E. coli ribosomes. All ribosomal proteins have been isolated and many specific antibodies have been produced. These, together with electronic microscopy and the use of certain reactives, have allowed for the determination of the topography of the proteins in the ribosome. 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. More recently, a near-complete (near)atomic picture of the ribosomal proteins is emerging from the latest high-resolution cryo-EM data.
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.
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).
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.
Ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. The 60S subunit is the large subunit of eukaryotic 80S ribosomes. It is structurally and functionally related to the 50S subunit of 70S prokaryotic ribosomes. However, the 60S subunit is much larger than the prokaryotic 50S subunit and contains many additional protein segments, as well as ribosomal RNA expansion segments.
EF-G is a prokaryotic elongation factor involved in protein 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.
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.
Translational regulation refers to the control of the levels of protein synthesized from its mRNA. This regulation is vastly important to the cellular response to stressors, growth cues, and differentiation. In comparison to transcriptional regulation, it results in much more immediate cellular adjustment through direct regulation of protein concentration. The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of peptide elongation, termination of protein synthesis, or ribosome biogenesis. While these general concepts are widely conserved, some of the finer details in this sort of regulation have been proven to differ between prokaryotic and eukaryotic organisms.
The term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles, cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric macromolecules. They are generally of more than one of these types, and the mixtures are defined spatially, and with regard to their underlying chemical composition and structure. Macromolecules are found in living and nonliving things, and are composed of many hundreds or thousands of atoms held together by covalent bonds; they are often characterized by repeating units. Assemblies of these can likewise be biologic or non-biologic, though the MA term is more commonly applied in biology, and the term supramolecular assembly is more often applied in non-biologic contexts. MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions, and can be in either non-repeating structures, or in repeating linear, circular, spiral, or other patterns. The process by which MAs are formed has been termed molecular self-assembly, a term especially applied in non-biologic contexts. A wide variety of physical/biophysical, chemical/biochemical, and computational methods exist for the study of MA; given the scale of MAs, efforts to elaborate their composition and structure and discern mechanisms underlying their functions are at the forefront of modern structure science.
In molecular biology, VAR1 protein domain, otherwise known as variant protein 1, is a ribosomal protein that forms part of the small ribosomal subunit in yeast mitochondria. Mitochondria possess their own ribosomes responsible for the synthesis of a small number of proteins encoded by the mitochondrial genome. VAR1 is the only protein in the yeast mitochondrial ribosome to be encoded in the mitochondria - the remaining approximately 80 ribosomal proteins are encoded in the nucleus. VAR1 along with 15S rRNA are necessary for the formation of mature 37S subunits.
Ada E. Yonath is an Israeli crystallographer best known for her pioneering work on the structure of the ribosome. She is the current director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly of the Weizmann Institute of Science.
50S ribosomal protein L25 is a protein that in Escherichia coli is encoded by the rplY gene.
Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.