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

Gebetsberger, Jennifer Viktoria; Wyss, Leander; Mleczko, Anna M.; Reuther, Julia; Polacek, Norbert (2016). A tRNA-derived fragment competes with mRNA for ribosome binding and regulates translation during stress. RNA biology, 14(10), pp. 1364-1373. Taylor and Francis 10.1080/15476286.2016.1257470

Preview

Text Gebetsberger Wyss et al_2016.pdf - Accepted Version Available under License Publisher holds Copyright. Download (1MB) | Preview

Posttranscriptional processing of RNA molecules is a common strategy to enlarge the structural and functional repertoire of RNomes observed in all three 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 to 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 messenger RNA 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.

Interest & Impact

Downloads

171 since deposited on 24 Jan 2017
31 in the past 12 months

Citations

5 Citations in Web of Science ®
6 Citations in Scopus

Search

in Google Scholar™

Services

Actions (login required)

Edit item

Actions (login required)

Edit item