Evidence map›Paper›PMID 28613431›Full record

ArticleMolecular microbiology2017

A conserved coiled-coil protein pair focuses the cytokinetic Z-ring in Caulobacter crescentus.

Selamawit Abi Woldemeskel, Ryan McQuillen, Alex M Hessel, Jie Xiao, Erin D Goley

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2017. 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
4.4field-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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. GTPase activity regulates FtsZ ring positioning inMolecular biology of the cell · 2024
    Article
  5. Article
  6. Article
  7. Investigation of Acid Tolerance Mechanism ofFoods (Basel, Switzerland) · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  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

5 authors at 1 institution in 1 country.

Selamawit Abi WoldemeskelDepartments of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Ryan McQuillenBiophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID http://orcid.org/0000-0002-0399-5248
Alex M HesselDepartments of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Jie XiaoBiophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Erin D GoleyDepartments of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID http://orcid.org/0000-0002-8518-2303
Johns Hopkins University · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Probing the structure, dynamics and function of the E. coli divisomeR01GM086447 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI XIAO, JIE · 2011 to 2019
$3.8M
Regulation and Mechanism of the C. Crescentus Cytokinetic RingR01GM108640 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GOLEY, ERIN D · 2015 to 2019
$1.6M
NIGMS NIH HHS R01 GM086447NIGMS NIH HHS R01 GM108640NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

The cytoskeletal GTPase FtsZ assembles at midcell, recruits the division machinery and directs envelope invagination for bacterial cytokinesis. ZapA, a conserved FtsZ-binding protein, promotes Z-ring stability and efficient division through a mechanism that is not fully understood. Here, we investigated the function of ZapA in Caulobacter crescentus. We found that ZapA is encoded in an operon with a small coiled-coil protein we named ZauP. ZapA and ZauP co-localized at the division site and were each required for efficient division. ZapA interacted directly with both FtsZ and ZauP. Neither ZapA nor ZauP influenced FtsZ dynamics or bundling, in vitro, however. Z-rings were diffuse in cells lacking zapA or zauP and, conversely, FtsZ was enriched at midcell in cells overproducing ZapA and ZauP. Additionally, FtsZ persisted at the poles longer when ZapA and ZauP were overproduced, and frequently colocalized with MipZ, a negative regulator of FtsZ polymerization. We propose that ZapA and ZauP promote efficient cytokinesis by stabilizing the midcell Z-ring through a bundling-independent mechanism. The zauPzapA operon is present in diverse Gram-negative bacteria, indicating a common mechanism for Z-ring assembly.

Indexed as

Amino Acid SequenceBacterial ProteinsCarrier ProteinsCaulobacter crescentusCell Cycle ProteinsCell DivisionCytokinesisCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsMicroscopy, FluorescenceModels, MolecularOperonProtein BindingProtein Structure, TertiaryBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsZapA protein, E coli

Identifiers

PMID28613431
PMCPMC5570653
OpenAlexW2624990648

What OpenQuestion holds

Textmetadata
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.