Evidence map›Paper›PMID 9003766›Full record

ArticleThe EMBO journal1996

Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.

D Missiakas, F Schwager, J M Betton, C Georgopoulos, S Raina

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 167 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Identification of Substrates of Cytoplasmic Peptidyl-ProlylInternational journal of molecular sciences · 2020
    Article
  10. The HslV Protease fromInternational journal of molecular sciences · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?International journal for parasitology. Drugs and drug resistance · 2012
    Review
  18. Article
  19. Article
  20. Paddling mechanism for the substrate translocation by AAA+ motor revealed by multiscale molecular simulations.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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 1 institution in 1 country.

D MissiakasCentre National de Recherche Scientifique, LIDSM-CBBM, Marseille, France.
F Schwager
J M Betton
C Georgopoulos
S Raina
Centre National pour la Recherche Scientifique et Technique (CNRST) · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock response in Escherichia coli is autoregulated. Consistent with this, mutations in certain heat shock genes, such as dnaK, dnaJ, grpE or htrC lead to a higher constitutive heat shock gene expression at low temperatures. A similar situation occurs upon accumulation of newly synthesized peptides released prematurely from the ribosomes by puromycin. We looked for gene(s) which, when present in multicopy, prevent the constitutive heat shock response associated with htrC mutant bacteria or caused by the presence of puromycin. One such locus was identified and shown to carry the recently sequenced hslV hslU (clpQ clpY) operon. HslV/ClpQ shares a very high degree of homology with members of the beta-type subunit, constituting the catalytic core of the 20S proteasome. HslU/ClpY is 50% identical to the ClpX protein of E. coli, which is known to present large polypeptides to its partner, the ATP-independent proteolytic enzyme ClpP. We show that, in vivo, HslV and HslU interact and participate in the degradation of abnormal puromycylpolypeptides. Biochemical evidence suggests that HslV/ClpQ is an efficient peptidase whose activity is enhanced by HslU/CIpY in the presence of ATP.

Indexed as

Endopeptidase ClpEscherichia coli ProteinsProtein FoldingSerine EndopeptidasesAdenosine TriphosphatasesATP-Dependent ProteasesCloning, MolecularConcanavalin ADrug Resistance, MicrobialEndopeptidasesEscherichia coliHeat-Shock ProteinsHydrolysisOperonPuromycinRecombinant ProteinsAdenosine TriphosphatasesATP-Dependent ProteasesClpYQ protease, E coliConcanavalin AEndopeptidase ClpEndopeptidasesEscherichia coli ProteinsHeat-Shock ProteinsPuromycinRecombinant ProteinsSerine Endopeptidases

Identifiers

PMID9003766
PMCPMC452516
OpenAlexW1463297302

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.