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Gene Review

cysS  -  cysteinyl-tRNA synthetase

Methanococcus maripaludis S2

 
 
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High impact information on cysS

  • An experimental system is provided by the recently discovered O-phosphoseryl-tRNA synthetase (SepRS), which acylates tRNA(Cys) with phosphoserine (Sep), and the well known cysteinyl-tRNA synthetase, which charges the same tRNA with cysteine [1].
  • We determined the identity elements of Methanocaldococcus jannaschii tRNA(Cys) in the aminoacylation reaction for the two Methanococcus maripaludis synthetases SepRS (forming Sep-tRNA(Cys)) and cysteinyl-tRNA synthetase (forming Cys-tRNA(Cys)) [1].
  • The canonical CysRS has a higher affinity for cysteine than ProCysRS, a reason why M. maripaludis may have acquired cysS by a late lateral gene transfer [2].
  • This intriguing enzyme may even perform its dual role in organisms that possess a canonical single-specificity cysteinyl-tRNA synthetase (CysRS), raising the question as to whether this latter aminoacyl-tRNA synthetase is indeed required for cell viability [2].

References

  1. Emergence of the universal genetic code imprinted in an RNA record. Hohn, M.J., Park, H.S., O'donoghue, P., Schnitzbauer, M., S??ll, D. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis. Stathopoulos, C., Kim, W., Li, T., Anderson, I., Deutsch, B., Palioura, S., Whitman, W., Söll, D. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
 
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