A tRNA-derived fragment competes with mRNA for ribosome binding and regulates translation during stress
Publisher DOI
PubMed ID
27892771
Abstract
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.
Date Issued
2016-11-28
Publication Type
Article
Subject(s)
Language(s)
en
Additional Credits
Journal
RNA biology
Publisher
Taylor and Francis
ISSN
1555-8584
Access(Rights)
open.access