Reprograming of sRNA target specificity by the leader peptide peTrpL in response to antibiotic exposure.

Autor:	Melior H; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Li S; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Stötzel M; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Maaß S; Institute of Microbiology, University of Greifswald, 17489 Greifswald, Germany., Schütz R; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Azarderakhsh S; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Shevkoplias A; Faculty of Biology and Biotechnology, Higher School of Economics, 117312 Moscow, Russia.; Institute for Information Transmission Problems (the Kharkevich Institute, RAS), 127051 Moscow, Russia., Barth-Weber S; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Baumgardt K; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany., Ziebuhr J; Institute of Medical Virology, University of Giessen, 35392 Giessen, Germany., Förstner KU; Data Science and Services, ZB MED - Information Centre for Life Sciences, 50931 Cologne, Germany., Chervontseva Z; Institute for Information Transmission Problems (the Kharkevich Institute, RAS), 127051 Moscow, Russia., Becher D; Institute of Microbiology, University of Greifswald, 17489 Greifswald, Germany., Evguenieva-Hackenberg E; Institute of Microbiology and Molecular Biology, University of Giessen, 35392 Giessen, Germany.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2021 Mar 18; Vol. 49 (5), pp. 2894-2915.
DOI:	10.1093/nar/gkab093
Abstrakt:	Trans-acting regulatory RNAs have the capacity to base pair with more mRNAs than generally detected under defined conditions, raising the possibility that sRNA target specificities vary depending on the specific metabolic or environmental conditions. In Sinorhizobium meliloti, the sRNA rnTrpL is derived from a tryptophan (Trp) transcription attenuator located upstream of the Trp biosynthesis gene trpE(G). The sRNA rnTrpL contains a small ORF, trpL, encoding the 14-aa leader peptide peTrpL. If Trp is available, efficient trpL translation causes transcription termination and liberation of rnTrpL, which subsequently acts to downregulate the trpDC operon, while peTrpL is known to have a Trp-independent role in posttranscriptional regulation of antibiotic resistance mechanisms. Here, we show that tetracycline (Tc) causes rnTrpL accumulation independently of Trp availability. In the presence of Tc, rnTrpL and peTrpL act collectively to destabilize rplUrpmA mRNA encoding ribosomal proteins L21 and L27. The three molecules, rnTrpL, peTrpL, and rplUrpmA mRNA, form an antibiotic-dependent ribonucleoprotein complex (ARNP). In vitro reconstitution of this ARNP in the presence of competing trpD and rplU transcripts revealed that peTrpL and Tc cause a shift of rnTrpL specificity towards rplU, suggesting that sRNA target prioritization may be readjusted in response to changing environmental conditions. (Oxford University Press 2021.)
Databáze:	MEDLINE
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