Evidence map›Paper›PMID 28623318›Full record

ArticleScientific reports2017

ZipA and FtsA* stabilize FtsZ-GDP miniring structures.

Yaodong Chen, Haiyan Huang, Masaki Osawa, Harold P Erickson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  2. Article
  3. Investigating the effect of bacteriophages on bacterial FtsZ localisation.Frontiers in cellular and infection microbiology · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. The cell division protein MinD fromThe Journal of biological chemistry · 2018
    Article
  12. Review
  13. Article
  14. 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 at 2 institutions in 2 countries.

Yaodong ChenKey Laboratory of Resources Biology and Biotechnology in Western China, Ministry of Education, College of Life Sciences, Northwest University, Xi'an, Shaanxi Province, 710069, P.R. China. ydchen@nwu.edu.cn.
Haiyan HuangKey Laboratory of Resources Biology and Biotechnology in Western China, Ministry of Education, College of Life Sciences, Northwest University, Xi'an, Shaanxi Province, 710069, P.R. China.
Masaki OsawaDepartment of Cell Biology, Duke University Medical Center, Durham, NC, 27710, USA.
Harold P EricksonDepartment of Cell Biology, Duke University Medical Center, Durham, NC, 27710, USA.
Duke University · USMinistry of Education of the People's Republic of China · CN

Funding

Structure and Assembly Dynamics of FtsZR01GM066014 · NIGMS · DUKE UNIVERSITY · PI ERICKSON, HAROLD P · 2002 to 2018
$7.5M
NIGMS NIH HHS R01 GM066014
6 · The paper itself

Abstract

The cytokinetic division ring of Escherichia coli comprises filaments of FtsZ tethered to the membrane by FtsA and ZipA. Previous results suggested that ZipA is a Z-ring stabilizer, since in vitro experiments it is shown that ZipA enhanced FtsZ assembly and caused the filaments to bundles. However, this function of ZipA has been challenged by recent studies. First, ZipA-induced FtsZ bundling was not significant at pH greater than 7. Second, some FtsA mutants, such as FtsA* were able to bypass the need of ZipA. We reinvestigated the interaction of FtsZ with ZipA in vitro. We found that ZipA not only stabilized and bundled straight filaments of FtsZ-GTP, but also stabilized the highly curved filaments and miniring structures formed by FtsZ-GDP. FtsA* had a similar stabilization of FtsZ-GDP minirings. Our results suggest that ZipA and FtsA* may contribute to constriction by stabilizing this miniring conformation.

Indexed as

Bacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsCytoskeletonEscherichia coli ProteinsGuanosine DiphosphateGuanosine TriphosphateProtein BindingProtein StabilityStructure-Activity RelationshipBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsZ protein, BacteriaGuanosine DiphosphateGuanosine TriphosphateZipA protein, E coli

Identifiers

PMID28623318
PMCPMC5473857
OpenAlexW2622629735

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.