Evidence map›Paper›PMID 22931116›Full record

ArticleMolecular microbiology2012

Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability.

An-Chun Chien, Shannon Kian Gharabiklou Zareh, Yan Mei Wang, Petra Anne Levin

Abstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. Metabolic engineering ofSynthetic and systems biotechnology · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Bacterial Cell Size: Multifactorial and Multifaceted.Annual review of microbiology · 2017
    Review
  15. Article
  16. Article
  17. Metabolism Shapes the Cell.Journal of bacteriology · 2017
    Review
  18. Article
  19. Article
  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

4 authors.

An-Chun ChienDepartment of Biology, Washington University, St. Louis, MO 63130, USA. plevin@wustl.edu
Shannon Kian Gharabiklou Zareh
Yan Mei Wang
Petra Anne Levin

Funding

TEMPORAL AND SPATIAL CONTROL OF B SUBTILIS CYTOKINESISR01GM064671 · NIGMS · WASHINGTON UNIVERSITY · PI LEVIN, PETRA ANNE · 2002 to 2016
$3.9M
NIGMS NIH HHS GM64671NIGMS NIH HHS R01 GM064671
6 · The paper itself

Abstract

How cells co-ordinate size with growth and development is a major, unresolved question in cell biology. In previous work we identified the glucosyltransferase UgtP as a division inhibitor responsible for increasing the size of Bacillus subtilis cells under nutrient-rich conditions. In nutrient-rich medium, UgtP is distributed more or less uniformly throughout the cytoplasm and concentrated at the cell poles and/or the cytokinetic ring. Under these conditions, UgtP interacts directly with FtsZ to inhibit division and increase cell size. Conversely, under nutrient-poor conditions, UgtP is sequestered away from FtsZ in punctate foci, and division proceeds unimpeded resulting in a reduction in average cell size. Here we report that nutrient-dependent changes in UgtP's oligomerization potential serve as a molecular rheostat to precisely co-ordinate B. subtilis cell size with nutrient availability. Our data indicate UgtP interacts with itself and the essential cell division protein FtsZ in a high-affinity manner influenced in part by UDP glucose, an intracellular proxy for nutrient availability. These findings support a model in which UDP-glc-dependent changes in UgtP's oligomerization potential shift the equilibrium between UgtP•UgtP and UgtP•FtsZ, fine-tuning the amount of FtsZ available for assembly into the cytokinetic ring and with it cell size.

Indexed as

Bacillus subtilisBacterial ProteinsCell DivisionCulture MediaCytoskeletal ProteinsGene Expression Regulation, BacterialGlucosyltransferasesProtein BindingUridine Diphosphate GlucoseBacterial ProteinsCulture MediaCytoskeletal ProteinsFtsZ protein, BacteriaGlucosyltransferasesUridine Diphosphate Glucose

Identifiers

PMID22931116
PMCPMC3480987

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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.