Evidence map›Paper›PMID 16109960›Full record

ArticleJournal of bacteriology2005

Presence of multiple sites containing polar material in spherical Escherichia coli cells that lack MreB.

Trine Nilsen, Arthur W Yan, Gregory Gale, Marcia B Goldberg

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. 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
5.4field-weighted citation impact, top 4% 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, 47 citations in OpenAlex.

  1. Journal of cell science · 2019
    Article
  2. Polar delivery ofProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Cellular polarity in prokaryotic organisms.Cold Spring Harbor perspectives in biology · 2009
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  20. The bacterial actin-like cytoskeleton.Microbiology and molecular biology reviews : MMBR · 2006
    Review
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 1 institution in 1 country.

Trine NilsenBacterial Pathogenesis Laboratories, University Park, 65 Landsdowne Street, Cambridge, MA 02139, USA.
Arthur W Yan
Gregory Gale
Marcia B Goldberg
Massachusetts General Hospital · US

Funding

MECHANISM AND FUNCTION OF UNIPOLARITY OF SHIGELLA ICSAR01AI035817 · NIAID · YESHIVA UNIVERSITY · PI GOLDBERG, MARCIA B · 1994 to 2009
$3.9M
NIAID NIH HHS AI035817NIAID NIH HHS R01 AI035817
6 · The paper itself

Abstract

In rod-shaped bacteria, certain proteins are specifically localized to the cell poles. The nature of the positional information that leads to the proper localization of these proteins is unclear. In a screen for factors required for the localization of the Shigella sp. actin assembly protein IcsA to the bacterial pole, a mutant carrying a transposon insertion in mreB displayed altered targeting of IcsA. The phenotype of cells containing a transposon insertion in mreB was indistinguishable from that of cells containing a nonpolar mutation in mreB or that of wild-type cells treated with the MreB inhibitor A22. In cells lacking MreB, a green fluorescent protein (GFP) fusion to a cytoplasmic derivative of IcsA localized to multiple sites. Secreted full-length native IcsA was present in multiple faint patches on the surfaces of these cells in a pattern similar to that seen for the cytoplasmic IcsA-GFP fusion. EpsM, the polar Vibrio cholerae inner membrane protein, also localized to multiple sites in mreB cells and colocalized with IcsA, indicating that localization to multiple sites is not unique to IcsA. Our results are consistent with the requirement, either direct or indirect, for MreB in the restriction of certain polar material to defined sites within the cell and, in the absence of MreB, with the formation of ectopic sites containing polar material.

Indexed as

Gene DeletionBacterial ProteinsBinding SitesDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGenetic Complementation TestMicroscopy, ConfocalMutagenesis, InsertionalPlasmidsRecombinant ProteinsTranscription FactorsBacterial ProteinsDNA-Binding ProteinsEscherichia coli ProteinsMreB protein, E coliRecombinant ProteinsTranscription FactorsvirG protein, Shigella flexneri

Identifiers

PMID16109960
PMCPMC1196171
OpenAlexW2111048966

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.