Dr. Peter Moore has studied the ribosome from the inside out. He studied its proteins, its RNA, and now its overall structure. And he has used just about every available structural technique--neutron scattering, NMR, and X-ray crystallography.
His work began 40 years ago when he was a graduate student at Harvard University. There he studied the mechanism of protein synthesis with Dr. James Watson and earned his Ph.D. in 1966. The year after his graduate studies began, his advisor won the Nobel Prize.
As a postdoctoral fellow with Dr. Alfred Tissieres at the University of Geneva, Dr. Moore joined the first successful effort to isolate and purify ribosomal proteins. He continued postdoctoral work with Dr. H.E. Huxley at the MRC Laboratory of Molecular Biology in Cambridge, England.
In 1969, Dr. Moore returned to Yale University, where he had earned his B.S. in biophysics 8 years earlier. He joined the Yale faculty and began the work for which he is best known--using neutron scattering to map proteins in the small ribosomal subunit of E. coli.
Dr. Moore has worked continuously for more than 30 years at Yale, where he is now an endowed professor of chemistry with a joint appointment in the Department of Molecular Biophysics and Biochemistry.
He has collaborated with his Yale colleague Dr. Thomas Steitz to determine the X-ray crystallographic structure of the large ribosomal subunit of
Haloarcula marismortui, a hardy, salt-loving bacterial strain isolated from the Dead Sea. Their study has now resulted in an atomic resolution structure that proves that the peptidyl transferase of the ribosome, the site where peptide bonds form, is composed entirely of rRNA. As has long been suspected, the ribosome is a ribozyme.
They published this structure at 2.4 angstrom resolution in the August 11, 2000 issue of
Science. This paper gives detailed structural information and provides more evidence for a theory that was initially counterintuitive and controversial--that in ribosomes, it is the RNA, rather than the proteins, that is responsible for catalysis. As has long been suspected, the ribosome is a ribozyme. The recent papers by Drs. Yonath and Ramakrishnan confirm this conclusion.
Dr. Moore is a member of the National Academy of Sciences and has received a number of other awards and honors, including a Guggenheim fellowship, during which he learned NMR from Dr. R.J.P. Williams at the University of Oxford, England. The work in his lab is now evenly divided between crystallography and NMR.
NIGMS has supported Dr. Moore's research since 1983.
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