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Science 7 November 2008:
Vol. 322. no. 5903, pp. 953 - 956
DOI: 10.1126/science.1164840
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Reports

Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome

Albert Weixlbaumer,* Hong Jin,* Cajetan Neubauer, Rebecca M. Voorhees, Sabine Petry,{dagger} Ann C. Kelley, Venki Ramakrishnan{ddagger}

The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.

Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.

* These authors contributed equally to this work.

{dagger} Present address: Department of Cellular and Molecular Pharmacology, University of California, San Francisco, 600 16th Street, San Francisco, CA 94158-2517, USA.

{ddagger} To whom correspondence should be addressed. E-mail: ramak{at}mrc-lmb.cam.ac.uk

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