Evidence map›Paper›PMID 26061894›Full record

ArticleMolecular microbiology2015

Helicobacter pylori CheZ(HP) and ChePep form a novel chemotaxis-regulatory complex distinct from the core chemotaxis signaling proteins and the flagellar motor.

Paphavee Lertsethtakarn, Michael R Howitt, Juan Castellon, Manuel R Amieva, Karen M Ottemann

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. TheJournal of bacteriology · 2026
    Article
  2. Reassessing the Standard Chemotaxis Framework for Understanding Biased Migration inAnnual review of chemical and biomolecular engineering · 2024
    Review
  3. Article
  4. Journal of bacteriology · 2024
    Article
  5. Bacterial flagella hijack type IV pili proteins to control motility.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. AApplied and environmental microbiology · 2018
    Article
  12. Review
  13. 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
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

5 authors at 2 institutions in 1 country.

Paphavee LertsethtakarnDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA, 95064, USA.
Michael R HowittDepartment of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Juan CastellonDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA, 95064, USA.
Manuel R AmievaDepartment of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Karen M OttemannDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA, 95064, USA.
University of California, Santa Cruz · USStanford University · US

Funding

Roles for Motility in Helicobactor pylori pathogenesisR01AI050000 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI OTTEMANN, KAREN M · 2002 to 2011
$3.6M
The Role of Chemotaxis in Helicobacter pylori Distribution in the HostR01DK101314 · NIDDK · UNIVERSITY OF OREGON · PI GUILLEMIN, KAREN J · 2014 to 2017
$1.3M
NIAID NIH HHS AI050000NIAID NIH HHS R01 AI050000NIDDK NIH HHS R01 DK101314
6 · The paper itself

Abstract

Chemotaxis is important for Helicobacter pylori to colonize the stomach. Like other bacteria, H. pylori uses chemoreceptors and conserved chemotaxis proteins to phosphorylate the flagellar rotational response regulator, CheY, and modulate the flagellar rotational direction. Phosphorylated CheY is returned to its non-phosphorylated state by phosphatases such as CheZ. In previously studied cases, chemotaxis phosphatases localize to the cellular poles by interactions with either the CheA chemotaxis kinase or flagellar motor proteins. We report here that the H. pylori CheZ, CheZ(HP), localizes to the poles independently of the flagellar motor, CheA, and all typical chemotaxis proteins. Instead, CheZ(HP) localization depends on the chemotaxis regulatory protein ChePep, and reciprocally, ChePep requires CheZ(HP) for its polar localization. We furthermore show that these proteins interact directly. Functional domain mapping of CheZ(HP) determined the polar localization motif lies within the central domain of the protein and that the protein has regions outside of the active site that participate in chemotaxis. Our results suggest that CheZ(HP) and ChePep form a distinct complex. These results therefore suggest the intriguing idea that some phosphatases localize independently of the other chemotaxis and motility proteins, possibly to confer unique regulation on these proteins' activities.

Indexed as

ChemotaxisSignal TransductionBacterial ProteinsFlagellaHelicobacter pyloriPhosphoric Monoester HydrolasesProtein MultimerizationBacterial ProteinsPhosphoric Monoester Hydrolases

Identifiers

PMID26061894
PMCPMC4677328
OpenAlexW1940238873

What OpenQuestion holds

Textmetadata
LicenceTDM
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.