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

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

Graduate School:

Graduate School for Cellular and Biomedical Sciences (GCB)

UniBE Contributor:

Gebetsberger, Jennifer Viktoria; Wyss, Leander; Reuther, Julia and Polacek, Norbert

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

1555-8584

Publisher:

Taylor and Francis

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

24 Jan 2017 10:08

Last Modified:

03 Dec 2017 02:07

Publisher DOI:

10.1080/15476286.2016.1257470

PubMed ID:

27892771

BORIS DOI:

10.7892/boris.92441

URI:

https://boris.unibe.ch/id/eprint/92441

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