A tRNA-derived fragment competes with mRNA for ribosome binding and regulates translation during stress. Issue 10 (3rd October 2017)

• Record Type: Journal Article
• Authors: Gebetsberger, Jennifer; Wyss, Leander; Mleczko, Anna M.; Reuther, Julia; Polacek, Norbert
• Is Part Of: RNA biology. Volume 14:Issue 10(2017)
• Page Start: 1364
• Page End: 1373
• Publication Date: 2017-10-03
• Subjects: Ribosome -- ribosome-associated ncRNA -- translation regulation -- tRNA-derived fragments; RNA -- Periodicals; Molecular biology -- Periodicals; Molecular biology; RNA; Periodicals; 572.8805
• DOI: 10.1080/15476286.2016.1257470
• Languages: English
• ISSNs: 1547-6286

Abstract

ABSTRACT: 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.