title: Cysteinyl-tRNA deacylation can be uncoupled from protein synthesis.
abstract: 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).
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland, United States of America.
authors.forename: Alexandre
authors.initials: A
authors.lastname: David
authors.forename: Suman R
authors.initials: SR
authors.lastname: Das
authors.forename: James S
authors.initials: JS
authors.lastname: Gibbs
authors.forename: Jack R
authors.initials: JR
authors.lastname: Bennink
authors.forename: Jonathan W
authors.initials: JW
authors.lastname: Yewdell
mesh_terms: D000215:Acylation; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D018053:Arsenites / Q000494:pharmacology; D003545:Cysteine / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D008856:Microscopy, Fluorescence; D014176:Protein Biosynthesis / Q000187:drug effects / Q000502:physiology*; D012350:RNA, Transfer, Cys / Q000378:metabolism*
chemical_list: D018053:Arsenites; D012350:RNA, Transfer, Cys; D000604:Amino Acyl-tRNA Synthetases; D003545:Cysteine; C015001:arsenite