Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma

Min Guo, Yeeting E. Chong, Ryan Shapiro, Kirk Beebe, Xiang-Lei Yang and Paul Schimmel ()
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Min Guo: The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Yeeting E. Chong: The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Ryan Shapiro: The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Kirk Beebe: The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Xiang-Lei Yang: The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Paul Schimmel: The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, California 92037, USA

Nature, 2009, vol. 462, issue 7274, 808-812

Abstract: Editorial changes Alanyl tRNA synthetases can sometimes bind a glycine or a serine, instead of alanine. This would cause mistranslation if a 'wrong' amino acid were then transferred from the synthetase active site onto a growing polypeptide chain. Guo et al. use crystal structures, mutant enzymes and kinetic analyses to discover why the enzyme has such a promiscuous specificity, and how this problem is overcome through the evolution of the editing protein, AlaXps.

Date: 2009
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DOI: 10.1038/nature08612

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