Evidence map›Paper›PMID 34270916›Full record

ArticleMolecular cell2021

CTP regulates membrane-binding activity of the nucleoid occlusion protein Noc.

Adam S B Jalal, Ngat T Tran, Ling J Wu, Karunakaran Ramakrishnan, Martin Rejzek, Giulia Gobbato, Clare E M Stevenson, David M Lawson, Jeff Errington, Tung B K Le

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

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  10. Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024
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  20. Relief of ParB autoinhibition byScience advances · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Adam S B JalalDepartment of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK.
Ngat T TranDepartment of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK.
Ling J WuCentre for Bacterial Cell Biology, Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
Karunakaran RamakrishnanDepartment of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK.
Martin RejzekChemistry Platform, John Innes Centre, Norwich, NR4 7UH, UK.
Giulia GobbatoDepartment of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK.
Clare E M StevensonDepartment of Biological Chemistry, John Innes Centre, Norwich, NR4 7UH, UK.
David M LawsonDepartment of Biological Chemistry, John Innes Centre, Norwich, NR4 7UH, UK.
Jeff ErringtonCentre for Bacterial Cell Biology, Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
Tung B K LeDepartment of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK. Electronic address: tung.le@jic.ac.uk.
John Innes Centre · GBNewcastle University · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/000C0683Wellcome Trust
6 · The paper itself

Abstract

ATP- and GTP-dependent molecular switches are extensively used to control functions of proteins in a wide range of biological processes. However, CTP switches are rarely reported. Here, we report that a nucleoid occlusion protein Noc is a CTPase enzyme whose membrane-binding activity is directly regulated by a CTP switch. In Bacillus subtilis, Noc nucleates on 16 bp NBS sites before associating with neighboring non-specific DNA to form large membrane-associated nucleoprotein complexes to physically occlude assembly of the cell division machinery. By in vitro reconstitution, we show that (1) CTP is required for Noc to form the NBS-dependent nucleoprotein complex, and (2) CTP binding, but not hydrolysis, switches Noc to a membrane-active state. Overall, we suggest that CTP couples membrane-binding activity of Noc to nucleoprotein complex formation to ensure productive recruitment of DNA to the bacterial cell membrane for nucleoid occlusion activity.

Indexed as

Bacillus subtilisBacterial ProteinsCell DivisionCell MembraneChromosomes, BacterialCytidine TriphosphateCytoskeletal ProteinsPyrophosphatasesBacterial ProteinsCTPaseCytidine TriphosphateCytoskeletal ProteinsPyrophosphatasesbacterial cell divisionCTPin vitro reconstitutionmembrane-binding proteinNocnucleoid occlusion proteinParBX-ray crystallography

Identifiers

PMID34270916
PMCPMC8429893
OpenAlexW3183130378

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.