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Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis (Cys-tRNA Deacylation Is Uncoupled from Translation)

PLoS ONE, 2012, Vol.7(3), p.e33072 [Peer Reviewed Journal]

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  • Title:
    Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis (Cys-tRNA Deacylation Is Uncoupled from Translation)
  • Author: David, Alexandre ; Das, Suman R ; Gibbs, James S ; Bennink, Jack R ; Yewdell, Jonathan W
  • Contributor: Pant, Harish (Editor)
  • Found In: PLoS ONE, 2012, Vol.7(3), p.e33072 [Peer Reviewed Journal]
  • Subjects: Research Article ; Biology ; Molecular Biology ; Biochemistry
  • Language: English
  • Description: Aminoacyl-tRNA synthetases (ARSs) are critical components of protein translation, providing ribosomes with aminoacyl-tRNAs. In return, ribosomes release uncharged tRNAs as ARS substrates. Here, we show that tRNA deacylation can be uncoupled from protein synthesis in an amino acid specific manner. While tRNAs coupled to radiolabeled Met, Leu Lys, or Ser are stable in cells following translation inhibition with arsenite, radiolabeled Cys is released from tRNA at a high rate. We discuss possible translation independent functions for tRNA Cys .
  • Identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0033072

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