Evidence map›Paper›PMID 25278020›Full record

ArticleThe Journal of biological chemistry2014

FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.

Yoshiharu Sato, Akiko Takaya, Chakib Mouslim, Kelly T Hughes, Tomoko Yamamoto

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein degradation by a component of the chaperonin-linked protease ClpP.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Filtering input fluctuations in intensity and in time underlies stochastic transcriptional pulses without feedback.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Yoshiharu SatoFrom the Department of Microbiology and Molecular Genetics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, 260-8675 Japan and.
Akiko TakayaFrom the Department of Microbiology and Molecular Genetics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, 260-8675 Japan and.
Chakib Mouslimthe Department of Biology, University of Utah, Salt Lake City, Utah 84112.
Kelly T Hughesthe Department of Biology, University of Utah, Salt Lake City, Utah 84112 kelly.hughes@utah.edu.
Tomoko YamamotoFrom the Department of Microbiology and Molecular Genetics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, 260-8675 Japan and tomoko-y@faculty.chiba-u.jp.

Funding

Coupling gene regulation to flagellar morphogenesisR01GM056141 · NIGMS · UNIVERSITY OF WASHINGTON · PI HUGHES, KELLY T · 1998 to 2023
$8.3M
NIGMS NIH HHS GM056141NIGMS NIH HHS R01 GM056141
6 · The paper itself

Abstract

We previously reported that the ClpXP ATP-dependent protease specifically recognizes and degrades the flagellar master transcriptional activator complex, FlhD4C2, to negatively control flagellar biogenesis. The flagellum-related protein, FliT, is also a negative regulator of flagellar regulon by inhibiting the binding of FlhD4C2 to the promoter DNA. We have found a novel pathway of FliT inhibition of FlhD4C2 activity connected to ClpXP proteolysis. An in vitro degradation assay using purified proteins shows that FliT selectively increases ClpXP proteolysis of the FlhC subunit in the FlhD4C2 complex. FliT behaves specifically to ClpXP-dependent proteolysis of FlhC. An in vitro interaction assay detects the ternary complex of FliT-FlhD4C2-ClpX. FliT promotes the affinity of ClpX against FlhD4C2 complex, whereas FliT does not directly interact with ClpX. Thus, FliT interacts with the FlhC in FlhD4C2 complex and increases the presentation of the FlhC recognition region to ClpX. The DNA-bound form of FlhD4C2 complex is resistant to ClpXP proteolysis. We suggest that the role of FliT in negatively controlling the flagellar gene expression involves increasing free molecules of FlhD4C2 sensitive to ClpXP proteolysis by inhibiting the binding to the promoter DNA as well as enhancing the selective proteolysis of FlhC subunit by ClpXP.

Indexed as

Bacterial ProteinsDNA, BacterialElectrophoresis, Polyacrylamide GelEndopeptidase ClpFlagellaMolecular ChaperonesMutationPromoter Regions, GeneticProtein BindingProtein SubunitsProteolysisRegulonSalmonella typhimuriumTrans-ActivatorsBacterial ProteinsDNA, BacterialEndopeptidase ClpfliT protein, BacteriaMolecular ChaperonesProtein SubunitsTrans-ActivatorsATPases Associated with Diverse Cellular Activities (AAA)ChaperoneGene RegulationProtein DegradationProteolysis

Identifiers

PMID25278020
PMCPMC4239645

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Registered trials

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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.