Literature DB >> 11904177

Cysteinyl-tRNA formation and prolyl-tRNA synthetase.

Clarisse Jacquin-Becker1, Ivan Ahel, Alexandre Ambrogelly, Benfang Ruan, Dieter Söll, Constantinos Stathopoulos.   

Abstract

Aminoacyl-tRNA (AA-tRNA) formation is a key step in protein biosynthesis. This reaction is catalyzed with remarkable accuracy by the AA-tRNA synthetases, a family of 20 evolutionarily conserved enzymes. The lack of cysteinyl-tRNA (Cys-tRNA) synthetase in some archaea gave rise to the discovery of the archaeal prolyl-tRNA (Pro-tRNA) synthetase, an enzyme capable of synthesizing Pro-tRNA and Cys-tRNA. Here we review our current knowledge of this fascinating process.

Entities:  

Keywords:  Non-programmatic

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Year:  2002        PMID： 11904177     DOI： 10.1016/s0014-5793(02)02331-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  4 in total

Review 1.  On the evolution of structure in aminoacyl-tRNA synthetases.

Authors:  Patrick O'Donoghue; Zaida Luthey-Schulten
Journal:  Microbiol Mol Biol Rev       Date:  2003-12       Impact factor: 11.056

2.  Evolutionary profiles from the QR factorization of multiple sequence alignments.

Authors:  Anurag Sethi; Patrick O'Donoghue; Zaida Luthey-Schulten
Journal:  Proc Natl Acad Sci U S A       Date:  2005-03-01       Impact factor: 11.205

3.  Structure of the prolyl-tRNA synthetase from the eukaryotic pathogen Giardia lamblia.

Authors:  Eric T Larson; Jessica E Kim; Alberto J Napuli; Christophe L M J Verlinde; Erkang Fan; Frank H Zucker; Wesley C Van Voorhis; Frederick S Buckner; Wim G J Hol; Ethan A Merritt
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2012-08-18

4.  Snapshots of a shrinking partner: Genome reduction in Serratia symbiotica.

Authors:  Alejandro Manzano-Marín; Amparo Latorre
Journal:  Sci Rep       Date:  2016-09-07       Impact factor: 4.379
  4 in total

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