Evidence map›Paper›PMID 21097616›Full record

ArticleJournal of bacteriology2011

A LytM domain dictates the localization of proteins to the mother cell-forespore interface during bacterial endospore formation.

Jeffrey Meisner, Charles P Moran

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024
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  17. Structure of components of an intercellular channel complex in sporulating Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Structure of the basal components of a bacterial transporter.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

2 authors at 1 institution in 1 country.

Jeffrey MeisnerDepartment of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Charles P Moran
Emory University · US

Funding

RNA POLYMERASE AND BACTERIAL DIFFERENTIATIONR01GM054395 · NIGMS · EMORY UNIVERSITY · PI MORAN, CHARLES P. · 1996 to 2012
$4.1M
NIGMS NIH HHS R01 GM054395
6 · The paper itself

Abstract

A large number of proteins are known to reside at specific subcellular locations in bacterial cells. However, the molecular mechanisms by which many of these proteins are anchored at these locations remains unclear. During endospore formation in Bacillus subtilis, several integral membrane proteins are located specifically at the interface of the two adjacent cells of the developing sporangium, the mother cell and forespore. The mother cell membrane protein SpoIIIAH recognizes the cell-cell interface through an interaction with the forespore membrane protein SpoIIQ, and then the other proteins are positioned there by the SpoIIIAH-SpoIIQ complex. In this study, we investigated the molecular mechanisms underlying the formation of the SpoIIIAH-SpoIIQ complex. Using gel filtration chromatography and isothermal titration calorimetry, we measured the binding parameters that characterize the SpoIIIAH-SpoIIQ interaction in vitro. We also demonstrated that the interaction of SpoIIIAH and SpoIIQ is governed by their YscJ and degenerate LytM domains, respectively. Therefore, the LytM domain of SpoIIQ provides the positional cue that dictates the localization of mother cell membrane proteins to the mother cell-forespore interface.

Indexed as

Bacillus subtilisBacterial ProteinsCalorimetryChromatography, GelMembrane ProteinsProtein BindingProtein Interaction MappingProtein MultimerizationProtein Structure, TertiarySpores, BacterialBacterial ProteinsMembrane Proteins

Identifiers

PMID21097616
PMCPMC3021227
OpenAlexW2123545486

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.