Evidence map›Paper›PMID 31840842›Full record

ArticleThe EMBO journal2020

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

Michaela Šiková, Jana Wiedermannová, Martin Převorovský, Ivan Barvík, Petra Sudzinová, Olga Kofroňová, Oldřich Benada, Hana Šanderová, Ciarán Condon, Libor Krásný

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 37 citations in OpenAlex.

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  10. The alternative sigma factor SigN ofJournal of bacteriology · 2023
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  13. CRISPRi screen for enhancing heterologous α-amylase yield in Bacillus subtilis.Journal of industrial microbiology & biotechnology · 2023
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Michaela ŠikováInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.
Jana WiedermannováInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.
Martin PřevorovskýDepartment of Cell Biology, Faculty of Science, Charles University, Prague, Czech Republic.
Ivan BarvíkDivision of Biomolecular Physics, Institute of Physics, Charles University, Prague 2, Czech Republic.
Petra SudzinováInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.
Olga KofroňováInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.
Oldřich BenadaInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.ORCID 0000-0002-4592-6216
Hana ŠanderováInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.
Ciarán CondonUMR8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, Paris, France.ORCID 0000-0002-2199-9621
Libor KrásnýInstitute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.ORCID 0000-0002-4120-4347
Czech Academy of Sciences · CZCharles University · CZCentre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche (ARNr-QC) and the Labex (Dynamo) programCzech Research Infrastructure for Systems Biology C4SYS LM2015055Czech Science Foundation 19-12956SCzech Science Foundation P305/12/G034Light Microscopy Core Facility, IMG ASCR, Prague, Czech Republic LM2015062Ministry of Education, Youth, and Sports of the Czech Republic LO1419Ministry of Education, Youth, and Sports of the Czech Republic LO1509OPPK CZ.2.16/3.1.00/21547
6 · The paper itself

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.

Indexed as

Bacillus subtilisBacterial ProteinsDNA-Directed RNA PolymerasesExoribonucleasesGene Expression Regulation, BacterialRNA, BacterialRNA, MessengerTranscription, GeneticBacterial ProteinsDNA-Directed RNA PolymerasesExoribonucleasesRNA, BacterialRNA, MessengerRNAPRNase J1stallingtorpedotranscription-replication collision

Identifiers

PMID31840842
PMCPMC6996504
OpenAlexW2995109237

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.