Peter B. Moore

Sterling Professor of Chemistry
Professor of Molecular Biophysics and Biochemistry
Member of Yale faculty since 1969

E-mail: peter.moore@yale.edu
Web site: http://www.yale.edu/moorelab

Research Since 1980, a host of RNAs have been identified that contribute to gene expression beyond the set identified 40 years ago: rRNAs, mRNAs, and tRNAs. The RNA world is far larger than anyone thought even as recently as ten years ago. While great progress has been made in the past decade, relative to what is known about proteins, our understanding of the structures of RNAs and the complexes it forms with proteins, and the relationship between RNA structure and the biological function, remains primitive. The goal of this laboratory, broadly speaking, is to contribute to the advance of this important field.

All of the work going on in the group today has to do with the ribosome one way or another. On the one hand, in collaboration with Professor T.A. Steitz, we continue to work on the structure of the ribosome and the complexes it forms with inhibitors. In much of this work we take advantage of the atomic resolution structure we obtained a few years for the large ribosomal subunit. Now, for the first time, we can determine the structural consequences of mutations in both rRNA and in ribosomal proteins in that system. On the other hand, we are studying the translational control of ribosomal protein synthesis in bacteria using NMR, crystallography and molecular biology as tools.

Education
B.S. Yale University, 1961
Ph.D. Harvard University, 1966
Postdoctoral Fellow, Institut de Biologie Moleculaire, University of Geneva (Switzerland), 1966-67
Medical Research Council Laboratory of Molecular Biology, Cambridge (UK), 1967-69

Honors
NIH Merit Award, 1986-95
Fellow of AAAS, 1992
National Academy of Sciences, 1997
Rosenstiel Award, 2001
AAAS Newcomb Cleveland Prize, 2002
American Academy of Arts and Sciences, 2003
Biophysical Society, Presdient-Elect, 2009

Recent Publications
S. Tu, G. Blaha, P.B. Moore, & T.A. Steitz. Structures of MLSbK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 2005, 121, 257-270.

N.R. Voss, M. Gerstein, T.A. Steitz, & P.B. Moore. The geometry of the ribosomal polypeptide exit tunnel. J. Mol. Biol. 2006, 360, 893-906.

H. Jin, J.P. Loria, & P.B. Moore. Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a box H/ACA snoRNA. Molec. Cell 2007, 26, 205-215.

S.J. Schroeder, G. Blaha, J. Tirado-Rives, T.A. Steitz, & P.B. Moore. The structure of antibiotics bound to the E site region of the 50S ribosomal subunit of Haloarcula marismortui: 13-deoxytedanolide and girodazole. J. Mol. Biol. 2007, 367, 1471-1479.

G. Blaha, G. Gurel, S.J. Schroeder, P.B. Moore, & T.A. Steitz. Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. J. Mol. Biol. 2008, 379, 505-519.

Peter B. Moore

Research Interests