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• W1596239314 abstract "Reconstitution of Escherichia coli 30 S Ribosomal Subunits from Purified Molecular Components (Held, W. A., Mizushima, S., and Nomura, M. (1973) J. Biol. Chem. 248, 5720–5730) Assembly Mapping of 30 S Ribosomal Proteins from Escherichia coli. Further Studies (Held, W. A., Ballou, B., Mizushima, S., and Nomura, M. (1974) J. Biol. Chem. 249, 3103–3111) Escherichia coli 30 S Ribosomal Proteins Uniquely Required for Assembly (Held, W. A., and Nomura, M. (1975) J. Biol. Chem. 250, 3179–3184) Masayasu Nomura was born in 1927, in Hyogo-ken, Japan. He earned his B.S. and Ph.D. in Microbiology at the University of Tokyo and completed postdoctoral work at the University of Illinois, Harvard University, and Purdue University. In 1963, Nomura joined the faculty of the University of Wisconsin's Department of Genetics and was promoted to full professor in 1966. By the early 1960s, many of the components of protein biosynthesis had been identified. The term “ribosome” had been introduced, and it was known that ribosomes were the sites where amino acids were assembled into proteins. It was also known that ribosomes were made up of a large subunit and a small subunit, each consisting of RNA and various proteins. What was not known was how the molecular components were assembled into ribosomes and how the assembled structures performed their functions. Working at the University of Wisconsin, Nomura discovered that by centrifuging bacterial ribosomal 50 S and 30 S subunits in CsCl he could dissociate them into smaller subparticles and proteins. The subparticles were inactive in protein synthesis, but when Nomura mixed the subparticles with the dissociated proteins, he found they assembled into an active ribosome (1Hosokawa K. Fujimura R.K. Nomura M. Reconstitution of functionally active ribosomes from inactive subparticles and proteins.Proc. Natl. Acad. Sci. U. S. A. 1966; 55: 198-204Crossref PubMed Scopus (65) Google Scholar). Several years later, Nomura and his colleagues reconstituted the small ribosomal subunit from purified RNA and ribosomal proteins, which is the subject of the first Journal of Biological Chemistry (JBC) Classic reprinted here. Before the publication of this paper, Nomura had reconstituted the 30 S subunit using purified 16 S RNA and a mixture of 30 S ribosomal proteins extracted from purified 30 S subunits. In this paper, Nomura and his colleagues separated and purified each of the proteins in the 30 S subunit and then reconstituted functionally active 30 S subunits from these purified components and 16 S RNA. This reconstitution proved that the necessary information for the assembly of active ribosomes was contained in their molecular components rather than in some extraneous factor. Next, Nomura turned his attention to mapping the assembly of the 30 S ribosome. He had found that the in vitro reconstitution of Escherichia coli 30 S subunits occurred in a sequential, cooperative fashion. Several proteins bound first to the 16 S RNA and then others. Finally, still other proteins bound to these proteins to form the final structure. From this, Nomura generated an “assembly map” showing the cooperative effects among the various 30 S ribosomal proteins in the assembly reaction (2Mizushima S. Nomura M. Assembly mapping of 30S ribosomal proteins from E. coli.Nature. 1970; 226: 1214-1218Crossref PubMed Scopus (397) Google Scholar). In the second JBC Classic, Nomura and his colleagues clarified some uncertainties in the initial map and presented a revised assembly map. In studying the assembly of the ribosome, Nomura found that several 30 S proteins had essential roles in the assembly of 30 S subunits. He believed that it was possible that some of the proteins that played important roles in ribosomal assembly did not have any role in the functional activities of the assembled 30 S subunits. In the final JBC Classic reprinted here, Nomura and his colleagues showed that two 30 S ribosomal proteins from E. coli play just such roles. They found that S16 was required only for the efficient assembly of 30 S subunits and did not appear to be directly involved in any known 30 S ribosomal function. S18 appeared to play major roles in the stabilization of ribosome structure but did not appear to be directly involved in polypeptide chain elongation. Nomura later went on to identify and isolate the genes encoding the 3 ribosomal RNAs and ribosomal proteins, well before the advent of modern recombinant DNA technology. In the late 1970s, he turned his attention to ribosome biogenesis in bacteria and to the formulation and testing of models for the regulation of ribosome synthesis. His most recent work is on the mechanism of synthesis of ribosomal RNA in yeast. Nomura was appointed Co-director of the Institute for Enzyme Research at the University of Wisconsin in 1970 and remained there until 1984 when he moved to the University of California, Irvine. He is currently the Grace Bell Professor of Biological Chemistry at UC Irvine. Nomura is the recipient of several awards including the 1971 National Academy of Sciences Award in Molecular Biology, the UC Irvine Distinguished Faculty Lectureship Award for Research (2000–2001), and the 2002 Abbott-American Society for Microbiology Lifetime Achievement Award. He is a Fellow of the American Academy of Microbiology and the American Association for the Advancement of Science and a member of the National Academy of Sciences." @default.
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• W1596239314 date "2007-04-01" @default.
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• W1596239314 title "Purification of the Components of the Ribosome and Reconstitution of Active Ribosomes: the Work of Masayasu Nomura" @default.
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