tRNA-derived fragments target the small ribosomal subunit to fine-tune translation

Gebetsberger, Jennifer Viktoria (14 June 2015). tRNA-derived fragments target the small ribosomal subunit to fine-tune translation (Unpublished). In: International Conference on the Long and the Short of Non-Coding RNAs. Chania, Crete, Greece. 14.–19.06.2015.

Post-transcriptional cleavage of RNA molecules to generate smaller fragments is a widespread mechanism that enlarges the structural and functional complexity of cellular RNomes. In particular, fragments deriving from both precursor and mature tRNAs represent one of the rapidly growing classes of post-transcriptional RNA pieces. Importantly, these tRNA-derived fragments (tRFs) possess distinct expression patterns, abundance, cellular localizations, or biological roles compared with their parental tRNA molecules [1]. Here we present evidence that tRFs from the archaeon Haloferax volcanii directly bind to ribosomes. In a previous genomic screen for ribosome-associated small RNAs we have identified a 26 residue long fragment originating from the 5’ part of valine tRNA (Val-tRF) to be by far the most abundant tRF in H. volcanii [2]. The Val-tRF is processed in a stress- dependent manner and was found to primarily target the small ribosomal subunit in vitro and in vivo. Translational activity was markedly reduced in the presence of Val-tRF, while control RNA fragments of similar length did not show inhibition of protein biosynthesis. Crosslinking experiments and subsequent primer extension analyses revealed the Val-tRF interaction site to surround the mRNA path in the 30S subunit. In support of this, binding experiments demonstrated that Val-tRF does compete with mRNAs for ribosome binding. Therefore this tRF represents a ribosome-associated non-protein-coding RNA (rancRNA) capable of regulating gene expression in H. volcanii under environmental stress conditions probably by fine-tuning the rate of protein production [3].

Item Type:

Conference or Workshop Item (Poster)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Gebetsberger, Jennifer Viktoria

Subjects:

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

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

28 Jan 2016 16:11

Last Modified:

28 Jan 2016 16:11

URI:

https://boris.unibe.ch/id/eprint/74855

Actions (login required)

Edit item Edit item
Provide Feedback