Evidence map›Paper›PMID 20497502›Full record

ArticleMolecular microbiology2010

DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus.

Andrea Möll, Susan Schlimpert, Ariane Briegel, Grant J Jensen, Martin Thanbichler

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 86 citations in OpenAlex.

  1. A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Andrea MöllMax Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Susan Schlimpert
Ariane Briegel
Grant J Jensen
Martin Thanbichler
Max Planck Institute for Terrestrial Microbiology · DECalifornia Institute of Technology · US

Funding

Structure and function of the prokaryotic cytoskeleton by electron cryotomographyR01AI067548 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI JENSEN, GRANT J · 2006 to 2010
$1.6M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI067548
6 · The paper itself

Abstract

In bacteria, cytokinesis is dependent on lytic enzymes that facilitate remodelling of the cell wall during constriction. In this work, we identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in vitro, and is recruited to the site of constriction through interaction with the cell division protein FtsN. Mutational analyses showed that the LysM domains are necessary and sufficient for localization of DipM, while its peptidase domain is essential for function. Consistent with a role in cell wall hydrolysis, DipM was found to interact with purified murein sacculi in vitro and to induce cell lysis upon overproduction. Its inactivation causes severe defects in outer membrane invagination, resulting in a significant delay between cytoplasmic compartmentalization and final separation of the daughter cells. Overall, these findings indicate that DipM is a periplasmic component of the C. crescentus divisome that facilitates remodelling of the peptidoglycan layer and, thus, coordinated constriction of the cell envelope during the division process.

Indexed as

Cell DivisionBacterial ProteinsCaulobacter crescentusCell Cycle ProteinsDNA, BacterialDNA Mutational AnalysisEndopeptidasesMembrane ProteinsMolecular Sequence DataPeptidoglycanPeriplasmic ProteinsProtein BindingProtein Structure, TertiarySequence Analysis, DNABacterial ProteinsCell Cycle ProteinsDNA, BacterialEndopeptidasesMembrane ProteinsPeptidoglycanPeriplasmic Proteins

Identifiers

PMID20497502
PMCPMC3057925
OpenAlexW1845620697

What OpenQuestion holds

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LicenceTDM
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.