An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes

Nature
C FàbregaP Schimmel

Abstract

Aminoacyl transfer RNA synthetases catalyse the first step of protein synthesis and establish the rules of the genetic code through the aminoacylation of tRNAs. There is a distinct synthetase for each of the 20 amino acids and throughout evolution these enzymes have been divided into two classes of ten enzymes each. These classes are defined by the distinct architectures of their active sites, which are associated with specific and universal sequence motifs. Because the synthesis of aminoacyl-tRNAs containing each of the twenty amino acids is a universally conserved, essential reaction, the absence of a recognizable gene for cysteinyl tRNA synthetase in the genomes of Archae such as Methanococcus jannaschii and Methanobacterium thermoautotrophicum has been difficult to interpret. Here we describe a different cysteinyl-tRNA synthetase from M. jannaschii and Deinococcus radiodurans and its characterization in vitro and in vivo. This protein lacks the characteristic sequence motifs seen in the more than 700 known members of the two canonical classes of tRNA synthetase and may be of ancient origin. The existence of this protein contrasts with proposals that aminoacylation with cysteine in M. jannaschii is an auxiliary function of a...Continue Reading

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Citations

Mar 21, 2002·FEBS Letters·Clarisse Jacquin-BeckerConstantinos Stathopoulos
May 30, 2007·Molecular BioSystems·Terry CathopoulisTamara L Hendrickson
Mar 16, 2005·DNA and Cell Biology·Luyang YuLihe Guo
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May 24, 2003·Cold Spring Harbor Symposia on Quantitative Biology·C StathopoulosD Söll
Jan 20, 2004·Journal of Bacteriology·Pierre-Marie AkochyJacques Lapointe
Aug 14, 2003·Genome Biology·Kira S Makarova, Eugene V Koonin
Apr 4, 2002·Proceedings of the National Academy of Sciences of the United States of America·Alexei I SlesarevSergei A Kozyavkin
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