| Literature DB >> 31840842 |
Michaela Šiková1, Jana Wiedermannová1, Martin Převorovský2, Ivan Barvík3, Petra Sudzinová1, Olga Kofroňová1, Oldřich Benada1, Hana Šanderová1, Ciarán Condon4, Libor Krásný1.
Abstract
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.Entities:
Keywords: zzm321990RNAPzzm321990; RNase J1; stalling; torpedo; transcription-replication collision
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Year: 2019 PMID: 31840842 PMCID: PMC6996504 DOI: 10.15252/embj.2019102500
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598