Evidence map›Paper›PMID 16428401›Full record

ArticleJournal of bacteriology2006

GTPase activity, structure, and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB.

Osigwe Esue, Denis Wirtz, Yiider Tseng

Abstract read
In one paragraph

Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Effect of A22 on the Conformation of Bacterial Actin MreB.International journal of molecular sciences · 2019
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Effects of polymerization and nucleotide identity on the conformational dynamics of the bacterial actin homolog MreB.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Article
  14. Article
  15. Review
  16. Cytoskeletal proteins of actinobacteria.International journal of cell biology · 2012
    Article
  17. Article
  18. Article
  19. Article
  20. The structure and function of bacterial actin homologs.Cold Spring Harbor perspectives in biology · 2010
    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

3 authors.

Osigwe EsueDepartment of Chemical and Biomolecular Engineering, University The Johns Hopkins University, Baltimore, MD 21218, USA.
Denis Wirtz
Yiider Tseng

Funding

Temporal and Spatial Control of the Cell Cycle in Caulobacter CrescentusR01GM065835 · NIGMS · YALE UNIVERSITY · PI JACOBS-WAGNER, CHRISTINE · 2003 to 2016
$3.7M
NIGMS NIH HHS GM065835NIGMS NIH HHS R01 GM065835
6 · The paper itself

Abstract

MreB, a major component of the recently discovered bacterial cytoskeleton, displays a structure homologous to its eukaryotic counterpart actin. Here, we study the assembly and mechanical properties of Thermotoga maritima MreB in the presence of different nucleotides in vitro. We found that GTP, not ADP or GDP, can mediate MreB assembly into filamentous structures as effectively as ATP. Upon MreB assembly, both GTP and ATP release the gamma phosphate at similar rates. Therefore, MreB is an equally effective ATPase and GTPase. Electron microscopy and quantitative rheology suggest that the morphologies and micromechanical properties of filamentous ATP-MreB and GTP-MreB are similar. In contrast, mammalian actin assembly is favored in the presence of ATP over GTP. These results indicate that, despite high structural homology of their monomers, T. maritima MreB and actin filaments display different assembly, morphology, micromechanics, and nucleotide-binding specificity. Furthermore, the biophysical properties of T. maritima MreB filaments, including high rigidity and propensity to form bundles, suggest a mechanism by which MreB helical structure may be involved in imposing a cylindrical architecture on rod-shaped bacterial cells.

Indexed as

ActinsAdenosine TriphosphateCell MembraneCytoskeletal ProteinsEscherichia coli ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesStructure-Activity RelationshipThermotoga maritimaActinsAdenosine TriphosphateCytoskeletal ProteinsEscherichia coli ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesMreB protein, E coli

Identifiers

PMID16428401
PMCPMC1347329

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.