Evidence map›Paper›PMID 12426352›Full record

ArticleJournal of bacteriology2002

Degradation of a Caulobacter soluble cytoplasmic chemoreceptor is ClpX dependent.

Isabel Potocka, Melanie Thein, Magne ØSterås, Urs Jenal, M R K Alley

Abstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016
    Review
  9. Article
  10. Internal sense of direction: sensing and signaling from cytoplasmic chemoreceptors.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  11. Article
  12. Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 2 countries.

Isabel PotockaDepartment of Biological Sciences, South Kensington Campus, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom.
Melanie Thein
Magne ØSterås
Urs Jenal
M R K Alley
Imperial College London · GBUniversity of Basel · CH

Funding

Wellcome Trust
6 · The paper itself

Abstract

In order to determine whether ClpXP-mediated proteolysis is a common mechanism used to regulate the chemotaxis machinery during the cell cycle of Caulobacter crescentus, we have characterized a soluble cytoplasmic chemoreceptor, McpB. The mcpB gene lies adjacent to the major chemotaxis operon, which encodes 12 chemotaxis proteins, including the membrane chemoreceptor McpA. Like McpA, McpB possesses a C-terminal CheBR docking motif and three potential methylation sites, which we suggest are methylated. The McpB protein is degraded via a ClpX-dependent pathway during the swarmer-to-stalked cell transition, and a motif, which is 3 amino acids N-terminal to the McpB CheBR docking site, is required for proteolysis. Analysis of the degradation signal in McpB and McpA reveals a common motif present in the other four chemoreceptors that possess CheBR docking sites. A green fluorescent protein (GFP) fusion bearing 58 amino acids from the C terminus of McpA, which contains this motif, is degraded, suggesting that the C-terminal sequence is sufficient to confer ClpXP protease susceptibility.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceATPases Associated with Diverse Cellular ActivitiesBacterial ProteinsCaulobacter crescentusCell CycleChemoreceptor CellsChemotaxisCytoplasmEndopeptidase ClpEscherichia coli ProteinsGene Expression Regulation, BacterialMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular ChaperonesMolecular Sequence DataAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesBacterial ProteinsClpX protein, E coliEndopeptidase ClpEscherichia coli ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular Chaperones

Identifiers

PMID12426352
PMCPMC135435
OpenAlexW2135086075

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.