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The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes

M. Šiková, J. Wiedermannová, M. Převorovský, I. Barvík, P. Sudzinová, O. Kofroňová, O. Benada, H. Šanderová, C. Condon, L. Krásný,

. 2020 ; 39 (3) : e102500. [pub] 20191216

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc20025207

Grantová podpora
LM2015055 Czech Research Infrastructure for Systems Biology C4SYS - International
LM2015062 Light Microscopy Core Facility, IMG ASCR, Prague, Czech Republic - International
CZ.2.16/3.1.00/21547 OPPK - International
LO1419 Ministry of Education, Youth, and Sports of the Czech Republic - International
LO1509 Ministry of Education, Youth, and Sports of the Czech Republic - International
P305/12/G034 Czech Science Foundation - International
19-12956S Czech Science Foundation - International
Agence Nationale de la Recherche (ARNr-QC) and the Labex (Dynamo) program - International

RNase J1 is the major 5'-to-3' bacterial exoribonuclease. We demonstrate that in its absence, RNA polymerases (RNAPs) are redistributed on DNA, with increased RNAP occupancy on some genes without a parallel increase in transcriptional output. This suggests that some of these RNAPs represent stalled, non-transcribing complexes. We show that RNase J1 is able to resolve these stalled RNAP complexes by a "torpedo" mechanism, whereby RNase J1 degrades the nascent RNA and causes the transcription complex to disassemble upon collision with RNAP. A heterologous enzyme, yeast Xrn1 (5'-to-3' exonuclease), is less efficient than RNase J1 in resolving stalled Bacillus subtilis RNAP, suggesting that the effect is RNase-specific. Our results thus reveal a novel general principle, whereby an RNase can participate in genome-wide surveillance of stalled RNAP complexes, preventing potentially deleterious transcription-replication collisions.

Citace poskytuje Crossref.org

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