A tRNA-derived fragment competes with mRNA for ribosome binding and regulates translation during stress

RNA Biol. 2017 Oct 3;14(10):1364-1373. doi: 10.1080/15476286.2016.1257470. Epub 2016 Nov 28.


Posttranscriptional processing of RNA molecules is a common strategy to enlarge the structural and functional repertoire of RNomes observed in all 3 domains of life. Fragmentation of RNA molecules of basically all functional classes has been reported to yield smaller non-protein coding RNAs (ncRNAs) that typically possess different roles compared with their parental transcripts. Here we show that a valine tRNA-derived fragment (Val-tRF) that is produced under certain stress conditions in the halophilic archaeon Haloferax volcanii is capable of binding to the small ribosomal subunit. As a consequence of Val-tRF binding mRNA is displaced from the initiation complex which results in global translation attenuation in vivo and in vitro. The fact that the archaeal Val-tRF also inhibits eukaryal as well as bacterial protein biosynthesis implies a functionally conserved mode of action. While tRFs and tRNA halves have been amply identified in recent RNA-seq project, Val-tRF described herein represents one of the first functionally characterized tRNA processing products to date.

Keywords: Ribosome; ribosome-associated ncRNA; tRNA-derived fragments; translation regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Gene Expression Regulation, Archaeal
  • Haloferax volcanii / chemistry
  • Haloferax volcanii / genetics*
  • Haloferax volcanii / metabolism
  • Models, Molecular
  • Protein Biosynthesis
  • RNA, Archaeal / metabolism
  • RNA, Messenger / chemistry
  • RNA, Messenger / metabolism*
  • RNA, Transfer, Val / chemistry
  • RNA, Transfer, Val / metabolism*
  • Ribosomes / chemistry
  • Ribosomes / metabolism*
  • Stress, Physiological


  • RNA, Archaeal
  • RNA, Messenger
  • RNA, Transfer, Val