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PETER MOORE

In the 1960s, when molecular biology first emerged as a recognized discipline, only three classes of RNAs were known: rRNAs, tRNAs, and mRNAs. In recent decades, many other kinds of RNAs have been discovered, siRNAs and related regulatory RNAs being only the most recent examples. They all make important contributions to gene expression in one way or another. The reason it took so long for these other kinds of RNAs to be identified is that most of them are present in cells in much lower abundance than molecules like ribosomal RNAs, and are many of them unique to eukaryotic cells, which molecular biologists for the most part ignored in the early years. Our understanding of RNA structure has not kept up with the growth in our understanding of what RNA contributes to cellular function, and for that reason determination of the structures of biologically interesting RNAs and ribonucleoproteins remains an important enterprise.

We pursue RNA structures both by high field NMR, and by X-ray crystallography, and we are also interested in the structures of proteins that interact with RNAs, and ribonucleoprotein structure. On the NMR side, for example, we are using both homonuclear and heteronuclear approaches to determine the structures of box H/ACA RNAs and the complexes they form with their rRNA substrates. The development of new techniques is also an interest.

On the crystallographic side, we continue to collaborate with Prof. T.A. Steitz on the determination of the three-dimensional structure of the ribosome, the complexes it forms with ligands like antibiotics, and the conformational effects of ribosomal mutations. The object we have been concentrating on is the large ribosomal subunit from the halophilic archaean Haloarcula marismortui, which we solved at a resolution of 2.4 Å in 2000. Efforts are also being made to determine the structure of eukaryotic ribosomes at atomic resolution.

Selected Publications
Vallurupalli, P. and Moore, P. B. The solution structure of the loop E region of 5S rRNA from spinach chloroplasts. J. Mol. Biol. 325, 843-856 (2003)

Schmeing, T. M., Moore, P. B. and Steitz, T. A. Structure of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA 9, 1345-1352 (2003)

Merianos, H., Wang, J. and Moore, P. B. The structure of a ribosomal protein S8/spc operon mRNA complex. RNA 10, 954-964 (2004)

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

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

Last Updated 12-18-06