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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 (mRNA) 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 (rRNA) molecules and many ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.
VenkatramanRamakrishnan is an Indian-born British and American structural biologist who shared the 2009 Nobel Prize in Chemistry with Thomas A. Steitz and Ada Yonath, "for studies of the structure and function of the ribosome".
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Joan Elaine Argetsinger Steitz is Sterling Professor of Molecular Biophysics and Biochemistry at Yale University and Investigator at the Howard Hughes Medical Institute. She is known for her discoveries involving RNA, including ground-breaking insights into how ribosomes interact with messenger RNA by complementary base pairing and that introns are spliced by small nuclear ribonucleic proteins (snRNPs), which occur in eukaryotes. In September 2018, Steitz won the Lasker-Koshland Award for Special Achievement in Medical Science. The Lasker award is often referred to as the 'American Nobel' because 87 of the former recipients have gone on to win Nobel prizes.
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.
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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.
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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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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.
The P-site is the second binding site for tRNA in the ribosome. The other two sites are the A-site (aminoacyl), which is the first binding site in the ribosome, and the E-site (exit), the third. During protein translation, the P-site holds the tRNA which is linked to the growing polypeptide chain. When a stop codon is reached, the peptidyl-tRNA bond of the tRNA located in the P-site is cleaved releasing the newly synthesized protein. During the translocation step of the elongation phase, the mRNA is advanced by one codon, coupled to movement of the tRNAs from the ribosomal A to P and P to E sites, catalyzed by elongation factor EF-G.
Wayne A. Hendrickson is an American biophysicist and University professor at Columbia. Dr. Hendrickson is a University Professor at Columbia University in the Department of Biochemistry and Molecular Biophysics and Violin Family Professor of Physiology and Cellular Biophysics. He is also Chief Life Scientist in the Photon Sciences Directorate at Brookhaven National Laboratory and Scientific Director of the New York Structural Biology Center. Hendrickson has a B.A. from the University of Wisconsin at River Falls, a Ph.D. in biophysics at Johns Hopkins University with Warner Love, and postdoctoral research experience with Jerome Karle at the Naval Research Laboratory (NRL). He and his colleagues use biochemistry and x-ray crystallography to study molecular properties in atomic detail with current emphasis on membrane receptors and cellular signaling, on viral proteins and HIV infection, on molecular chaperones and protein folding, and on structural genomics of membrane proteins. Hendrickson's advances in diffraction methodology have contributed significantly to the emergence of structural biology as a major force in modern biology and molecular medicine.
Jennifer Anne Doudna is an American biochemist who has done pioneering work in CRISPR gene editing, and made other fundamental contributions in biochemistry and genetics. Doudna was one of the first women to share a Nobel in the sciences. She received the 2020 Nobel Prize in Chemistry, with Emmanuelle Charpentier, "for the development of a method for genome editing." She is the Li Ka Shing Chancellor's Chair Professor in the Department of Chemistry and the Department of Molecular and Cell Biology at the University of California, Berkeley. She has been an investigator with the Howard Hughes Medical Institute since 1997.
Ada E. Yonath is an Israeli crystallographer 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.
Nenad Ban is a Croatian biochemist born in Zagreb, Croatia who currently works at the ETH Zurich, Swiss Federal Institute of Technology, as a professor of Structural Molecular Biology.
Lynne Elizabeth Maquat is an American biochemist and molecular biologist whose research focuses on the cellular mechanisms of human disease. She is an elected member of the American Academy of Arts and Sciences, the National Academy of Sciences and the National Academy of Medicine. She currently holds the J. Lowell Orbison Endowed Chair and is a professor of biochemistry and biophysics, pediatrics and of oncology at the University of Rochester Medical Center. Professor Maquat is also Founding Director of the Center for RNA Biology and Founding Chair of Graduate Women in Science at the University of Rochester.
Rachel Green is a Bloomberg Distinguished Professor of molecular biology and genetics at the Johns Hopkins University School of Medicine. Her research focuses on ribosomes and their function in translation. Green has also been a Howard Hughes Medical Institute investigator since 2000.
References
- 1 2 3 "Harry F. Noller, Ph.D." The Gairdner Awards. Archived from the original on 1 August 2009. Retrieved 11 January 2011.
- 1 2 Soo Hoo Lee (2013-12-01). "Harry F. Nollder's Reflections". ASBMB Today (a publication of the American Society for Biochemistry and Molecular Biology). Archived from the original on 2019-11-01. Retrieved 2019-02-28.
{{cite journal}}: Cite journal requires|journal=(help) - 1 2 3 "UCSC biologist Harry Noller honored by Paul Ehrlich Foundation". University News & Events. University of California. Retrieved 11 January 2011.
- ↑ HF Noller, V Hoffarth, and L Zimniak. Unusual resistance of peptidyl transferase to protein extraction procedures; Science 256:5062, 1416-1419
- ↑ JH Cate, MM Yusupov, GZ Yusupova, TN Earnest, HF Noller, X-ray Crystal Structures of 70S Ribosome Functional Complexes Science 285:5436, 2095 - 2104
- ↑ MM Yusupov, GZ Yusupova, A Baucom, K Lieberman, TN Earnest, JHD Cate, HF Noller, Crystal Structure of the Ribosome at 5.5 Å Resolution Science 292:5518, 883 - 896
- ↑ Nicholson, Josh (May 24, 2007). "Harry Noller Wins Award for Ribosome Work". City on a Hill Press. Retrieved 11 January 2011.
- ↑ "5 top scientists win Breakthrough Prizes in star-studded event". 5 December 2016.
