Evidence map›Paper›PMID 21097625›Full record

ArticleJournal of bacteriology2011

Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli.

Bang Shen, Joe Lutkenhaus

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Investigating the effect of bacteriophages on bacterial FtsZ localisation.Frontiers in cellular and infection microbiology · 2022
    Article
  2. The Division Defect of aJournal of bacteriology · 2021
    Article
  3. Article
  4. Review
  5. 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

2 authors at 1 institution in 1 country.

Bang ShenDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, USA.
Joe Lutkenhaus
University of Kansas Medical Center · US

Funding

REGULATION OF CELL DIVISIONR37GM029764 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LUTKENHAUS, JOSEPH F · 2000 to 2010
$4.8M
REGULATION OF EXPRESSION OF CELL DIVISION GENESR01GM029764 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LUTKENHAUS, JOSEPH F · 1985 to 2022
$4.2M
NIGMS NIH HHS GM029764NIGMS NIH HHS R01 GM029764NIGMS NIH HHS R37 GM029764
6 · The paper itself

Abstract

In Escherichia coli the Z ring has the potential to assemble anywhere along the cell length but is restricted to midcell by the action of negative regulatory systems, including Min. In the current model for the Min system, the MinC/MinD division inhibitory complex is evenly distributed on the membrane and can disrupt Z rings anywhere in the cell; however, MinE spatially regulates MinC/MinD by restricting it to the cell poles, thus allowing Z ring formation at midcell. This model assumes that Z rings formed at different cellular locations have equal sensitivity to MinC/MinD in the absence of MinE. However, here we report evidence that differences in MinC/MinD sensitivity between polar and nonpolar Z rings exists even when there is no MinE. MinC/MinD at proper levels is able to block minicell production in Δmin strains without increasing the cell length, indicating that polar Z rings are preferentially blocked. In the FtsZ-I374V strain (which is resistant to MinC(C)/MinD), wild-type morphology can be easily achieved with MinC/MinD in the absence of MinE. We also show that MinC/MinD at proper levels can rescue the lethal phenotype of a min slmA double deletion mutant, which we think is due to the elimination of polar Z rings (or FtsZ structures), which frees up FtsZ molecules for assembly of Z rings at internal sites to rescue division and growth. Taken together, these data indicate that polar Z rings are more susceptible to MinC/MinD than internal Z rings, even when MinE is absent.

Indexed as

Cell DivisionProtein MultimerizationAdenosine TriphosphatasesBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsMembrane ProteinsMicroscopyAdenosine TriphosphatasesBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaMembrane ProteinsMinC protein, E coliMinD protein, E coliMinE protein, E coli

Identifiers

PMID21097625
PMCPMC3019829
OpenAlexW2097423909

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.