Evidence map›Paper›PMID 20497335›Full record

ArticleMolecular microbiology2010

A remote CheZ orthologue retains phosphatase function.

Paphavee Lertsethtakarn, Karen M Ottemann

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Journal of bacteriology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. AApplied and environmental microbiology · 2018
    Article
  10. Review
  11. Cooperation of two distinct coupling proteins creates chemosensory network connections.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. A Single-cell genome for Thiovulum sp.Applied and environmental microbiology · 2012
    Article
  16. Chemotaxis in Campylobacter jejuni.European journal of microbiology & immunology · 2012
    Review
  17. Article
  18. Review
  19. Article
  20. Conserved mechanism for sensor phosphatase control of two-component signaling revealed in the nitrate sensor NarX.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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.

Paphavee LertsethtakarnDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.
Karen M Ottemann
University of California, Santa Cruz · US

Funding

Roles for Motility in Helicobactor pylori pathogenesisR01AI050000 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI OTTEMANN, KAREN M · 2002 to 2011
$3.6M
NIAID NIH HHS R01 AI050000
6 · The paper itself

Abstract

Aspartyl-phosphate phosphatases underlie the rapid responses of bacterial chemotaxis. One such phosphatase, CheZ, was originally proposed to be restricted to beta and gamma proteobacter, suggesting only a small subset of microbes relied on this protein. A putative CheZ phosphatase was identified genetically in the epsilon proteobacter Helicobacter pylori (Mol Micro 61:187). H. pylori utilizes a chemotaxis system consisting of CheAY, three CheVs, CheW, CheY(HP) and the putative CheZ to colonize the host stomach. Here we investigate whether this CheZ has phosphatase activity. We phosphorylated potential targets in vitro using either a phosphodonor or the CheAY kinase and [gamma-(32)P]-ATP, and found that H. pylori CheZ (CheZ(HP)) efficiently dephosphorylates CheY(HP) and CheAY and has additional weak activity on CheV2. We detected no phosphatase activity towards CheV1 or CheV3. Mutations corresponding to Escherichia coli CheZ active site residues or deletion of the C-terminal region inactivate CheZ(HP) phosphatase activity, suggesting the two CheZs function similarly. Bioinformatics analysis suggests that CheZ phosphatases are found in all proteobacteria classes, as well as classes Aquificae, Deferribacteres, Nitrospira and Sphingobacteria, demonstrating that CheZ phosphatases are broadly distributed within Gram-negative bacteria.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCatalytic DomainComputational BiologyDNA, BacterialEscherichia coli ProteinsHelicobacter pyloriMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPhosphatesPhosphoric Monoester HydrolasesSequence Analysis, DNASequence Deletionaspartyl phosphate phosphataseBacterial ProteinscheY protein, E coliDNA, BacterialEscherichia coli ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMutant ProteinsPhosphatesPhosphoric Monoester Hydrolases

Identifiers

PMID20497335
PMCPMC2907456
OpenAlexW2151127781

What OpenQuestion holds

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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.