Evidence map›Paper›PMID 18812514›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

A channel connecting the mother cell and forespore during bacterial endospore formation.

Jeffrey Meisner, Xin Wang, Monica Serrano, Adriano O Henriques, Charles P Moran

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

72 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024
    Review
  8. Article
  9. Review
  10. High Resolution Analysis of Proteome Dynamics duringInternational journal of molecular sciences · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Milestones inMicrobial cell (Graz, Austria) · 2020
    Review
  16. Article
  17. Review
  18. Bacterial Spore mRNA - What's Up With That?Frontiers in microbiology · 2020
    Review
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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.

Jeffrey MeisnerDepartment of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Xin Wang
Monica Serrano
Adriano O Henriques
Charles P Moran
Emory University · USUniversidade Nova de Lisboa · PT

Funding

RNA POLYMERASE AND BACTERIAL DIFFERENTIATIONR01GM054395 · NIGMS · EMORY UNIVERSITY · PI MORAN, CHARLES P. · 1996 to 2012
$4.1M
NIGMS NIH HHS GM54395NIGMS NIH HHS R01 GM054395
6 · The paper itself

Abstract

At an early stage during Bacillus subtilis endospore development the bacterium divides asymmetrically to produce two daughter cells. The smaller cell (forespore) differentiates into the endospore, while the larger cell (mother cell) becomes a terminally differentiated cell that nurtures the developing forespore. During development the mother cell engulfs the forespore to produce a protoplast, surrounded by two bilayer membranes, which separate it from the cytoplasm of the mother cell. The activation of sigma(G), which drives late gene expression in the forespore, follows forespore engulfment and requires expression of the spoIIIA locus in the mother cell. One of the spoIIIA-encoded proteins SpoIIIAH is targeted specifically to the membrane surrounding the forespore, through an interaction of its C-terminal extracellular domain with the C-terminal extracellular domain of the forespore membrane protein SpoIIQ. We identified a homologous relationship between the C-terminal domain of SpoIIIAH and the YscJ/FliF protein family, members of which form multimeric rings involved in type III secretion systems and flagella. If SpoIIIAH forms a similar ring structure, it may also form a channel between the mother cell and forespore membranes. To test this hypothesis we developed a compartmentalized biotinylation assay, which we used to show that the C-terminal extracellular domain of SpoIIIAH is accessible to enzymatic modification from the forespore cytoplasm. These and other results lead us to suggest that SpoIIIAH forms part of a channel between the forespore and mother cell that is required for the activation of sigma(G).

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsBiotinylationCarbon-Nitrogen LigasesCytoplasmEscherichia coli ProteinsGene Expression RegulationMembrane ProteinsMolecular Sequence DataRepressor ProteinsSequence Homology, Amino AcidSigma FactorSpores, BacterialBacterial ProteinsbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli ProteinsFlif protein, BacteriaMembrane ProteinsRepressor ProteinsSigma Factorspore-specific proteins, Bacillus

Identifiers

PMID18812514
PMCPMC2567499
OpenAlexW1993304095

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.