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

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author J Gebetsberger, L Wyss, AM Mleczko, J Reuther, N Polacek,
Project Stress-mediated effects on ribosome functions and translation control
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Original article (peer-reviewed)

Journal RNA biology
Page(s) 1364
Title of proceedings RNA biology
DOI 10.1080/15476286.2016.1257470

Open Access

Type of Open Access Publisher (Gold Open Access)


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.