Evidence map›Paper›PMID 27381174›Full record

ArticleMolecular microbiology2016

GerM is required to assemble the basal platform of the SpoIIIA-SpoIIQ transenvelope complex during sporulation in Bacillus subtilis.

Christopher D A Rodrigues, Fernando H Ramírez-Guadiana, Alexander J Meeske, Xindan Wang, David Z Rudner

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Milestones inMicrobial cell (Graz, Austria) · 2020
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Vegetative Cell and Spore Proteomes ofJournal of proteome research · 2019
    Article
  19. Review
  20. 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

5 authors at 2 institutions in 2 countries.

Christopher D A RodriguesDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA, 02115, USA.
Fernando H Ramírez-GuadianaDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA, 02115, USA.
Alexander J MeeskeDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA, 02115, USA.
Xindan WangDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA, 02115, USA.
David Z RudnerDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA, 02115, USA. rudner@hms.harvard.edu.
Harvard University · USLouis Pasteur Center for Medical Research · JP

Funding

Membrane Remodeling and Protein Trafficking in BacteriaR01GM073831 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RUDNER, DAVID Z · 2005 to 2014
$3.4M
A multidisciplinary approach to elucidating gene function in a model Gram-positivRC2GM092616 · NIGMS · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2009 to 2010
$2.0M
NIGMS NIH HHS R01 GM073831NIGMS NIH HHS RC2 GM092616
6 · The paper itself

Abstract

Sporulating Bacillus subtilis cells assemble a multimeric membrane complex connecting the mother cell and developing spore that is required to maintain forespore differentiation. An early step in the assembly of this transenvelope complex (called the A-Q complex) is an interaction between the extracellular domains of the forespore membrane protein SpoIIQ and the mother cell membrane protein SpoIIIAH. This interaction provides a platform onto which the remaining components of the complex assemble and also functions as an anchor for cell-cell signalling and morphogenetic proteins involved in spore development. SpoIIQ is required to recruit SpoIIIAH to the sporulation septum on the mother cell side; however, the mechanism by which SpoIIQ specifically localizes to the septal membranes on the forespore side has remained enigmatic. Here, we identify GerM, a lipoprotein previously implicated in spore germination, as the missing factor required for SpoIIQ localization. Our data indicate that GerM and SpoIIIAH, derived from the mother cell, and SpoIIQ, from the forespore, have reciprocal localization dependencies suggesting they constitute a tripartite platform for the assembly of the A-Q complex and a hub for the localization of mother cell and forespore proteins.

Indexed as

Bacillus subtilisBacterial ProteinsLipoproteinsMembrane ProteinsProtein BindingSpores, BacterialBacterial ProteinsLipoproteinsMembrane Proteinsspore-specific proteins, Bacillus

Identifiers

PMID27381174
PMCPMC5055438
OpenAlexW2466524217

What OpenQuestion holds

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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.