Evidence map›Paper›PMID 24945826›Full record

ArticlePloS one2014

Structure of CbpA J-domain bound to the regulatory protein Cbpm explains its specificity and suggests evolutionary link between Cbpm and transcriptional regulators.

Naghmeh S Sarraf, Rong Shi, Laura McDonald, Jason Baardsnes, Linhua Zhang, Miroslaw Cygler, Irena Ekiel

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

10 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  7. TheMicroorganisms · 2020
    Article
  8. Article
  9. Article
  10. 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

7 authors at 4 institutions in 1 country.

Naghmeh S SarrafDepartment of Chemistry and Biochemistry, Concordia University, Montréal, Québec, Canada; Life Sciences, National Research Council of Canada, Montréal, Québec, Canada.
Rong ShiDépartement de biochimie, de microbiologie et de bio-informatique, et L'Institut de biologie intégrative et des systèmes, et PROTEO, Université Laval, Québec City, Québec, Canada.
Laura McDonaldDepartment of Chemistry and Biochemistry, Concordia University, Montréal, Québec, Canada; Life Sciences, National Research Council of Canada, Montréal, Québec, Canada.
Jason BaardsnesLife Sciences, National Research Council of Canada, Montréal, Québec, Canada.
Linhua ZhangDepartment of Biochemistry, McGill University, Montréal, Québec, Canada.
Miroslaw CyglerDepartment of Biochemistry, McGill University, Montréal, Québec, Canada; Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.
Irena EkielDepartment of Chemistry and Biochemistry, Concordia University, Montréal, Québec, Canada; Life Sciences, National Research Council of Canada, Montréal, Québec, Canada.
National Research Council Canada · CAMcGill University · CAConcordia University · CAUniversité Laval · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CbpA is one of the six E. coli DnaJ/Hsp40 homologues of DnaK co-chaperones and the only one that is additionally regulated by a small protein CbpM, conserved in γ-proteobacteria. CbpM inhibits the co-chaperone and DNA binding activities of CbpA. This regulatory function of CbpM is accomplished through reversible interaction with the N-terminal J-domain of CbpA, which is essential for the interaction with DnaK. CbpM is highly specific for CbpA and does not bind DnaJ despite the high degree of structural and functional similarity between the J-domains of CbpA and DnaJ. Here we report the crystal structure of the complex of CbpM with the J-domain of CbpA. CbpM forms dimers and the J-domain of CbpA interacts with both CbpM subunits. The CbpM-binding surface of CbpA is highly overlapping with the CbpA interface for DnaK, providing a competitive model for regulation through forming mutually exclusive complexes. The structure also provides the explanation for the strict specificity of CbpM for CbpA, which we confirmed by making mutants of DnaJ that became regulated by CbpM. Interestingly, the structure of CbpM reveals a striking similarity to members of the MerR family of transcriptional regulators, suggesting an evolutionary connection between the functionally distinct bacterial co-chaperone regulator CbpM and the transcription regulator HspR.

Indexed as

Evolution, MolecularAdenosine TriphosphatasesAmino Acid SequenceCarrier ProteinsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein EngineeringProtein Structure, TertiarySequence AlignmentSurface Plasmon ResonanceTrans-ActivatorsAdenosine TriphosphatasesCarrier ProteinsCbpA protein, E coliCbpM protein, E colidnaK protein, E coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsTrans-Activators

Identifiers

PMID24945826
PMCPMC4063869
OpenAlexW1996114974

What OpenQuestion holds

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LicenceCC BY
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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.