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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00524333" target="_blank" >RIV/61388971:_____/20:00524333 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/20:10414337 RIV/00216208:11320/20:10414337

Výsledek na webu

<a href="https://www.embopress.org/doi/abs/10.15252/embj.2019102500" target="_blank" >https://www.embopress.org/doi/abs/10.15252/embj.2019102500</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.15252/embj.2019102500" target="_blank" >10.15252/embj.2019102500</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

EMBO Journal

ISSN

0261-4189

e-ISSN

—

Svazek periodika

39

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

17

Strana od-do

e102500

Kód UT WoS článku

000502667400001

EID výsledku v databázi Scopus

2-s2.0-85076793026