Evidence map›Paper›PMID 11689685›Full record

ArticleMolecular and cellular biology2001

The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme.

T Hon, H C Lee, A Hach, J L Johnson, E A Craig, H Erdjument-Bromage, P Tempst, L Zhang

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

21 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Tetrapyrrole-based drought stress signalling.Plant biotechnology journal · 2015
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. The role of PAS kinase in PASsing the glucose signal.Sensors (Basel, Switzerland) · 2010
    Review
  11. Article
  12. Article
  13. Article
  14. Regulation of the HAP1 gene involves positive actions of histone deacetylases.Biochemical and biophysical research communications · 2007
    Article
  15. Article
  16. Article
  17. Characterization and prediction of protein-protein interactions within and between complexes.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

8 authors at 3 institutions in 1 country.

T HonDepartment of Biochemistry, NYU School of Medicine, New York, New York 10016, USA.
H C Lee
A Hach
J L Johnson
E A Craig
H Erdjument-Bromage
P Tempst
L Zhang
New York University · USMemorial Sloan Kettering Cancer Center · USUniversity of Wisconsin–Madison · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
MECHANISMS OF HEME SIGNALING IN EUKARYOTIC CELLSR01GM053453 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ZHANG, LI · 1997 to 2001
$477k
NCI NIH HHS P30 CA008748NCI NIH HHS P30 CA08748NIGMS NIH HHS GM53453
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, heme directly mediates the effects of oxygen on transcription through the heme activator protein Hap1. In the absence of heme, Hap1 is bound by at least four cellular proteins, including Hsp90 and Ydj1, forming a higher-order complex, termed HMC, and its activity is repressed. Here we purified the HMC and showed by mass spectrometry that two previously unidentified major components of the HMC are the Ssa-type Hsp70 molecular chaperone and Sro9 proteins. In vivo functional analysis, combined with biochemical analysis, strongly suggests that Ssa proteins are critical for Hap1 repression in the absence of heme. Ssa may repress the activities of both Hap1 DNA-binding and activation domains. The Ssa cochaperones Ydj1 and Sro9 appear to assist Ssa in Hap1 repression, and only Ydj1 residues 1 to 172 containing the J domain are required for Hap1 repression. Our results suggest that Ssa-Ydj1 and Sro9 act together to mediate Hap1 repression in the absence of heme and that molecular chaperones promote heme regulation of Hap1 by a mechanism distinct from the mechanism of steroid signaling.

Indexed as

DNA-Binding ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsBlotting, WesternFungal ProteinsGene Expression Regulation, FungalHeat-Shock ProteinsHemeHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMacromolecular SubstancesMass SpectrometryMicrofilament ProteinsMolecular ChaperonesMutationRepressor ProteinsDNA-Binding ProteinsFungal ProteinsHAP1 protein, S cerevisiaeHeat-Shock ProteinsHemeHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMacromolecular SubstancesMicrofilament ProteinsMolecular ChaperonesRepressor ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSRO9 protein, S cerevisiaeSSA2 protein, S cerevisiaeSSA3 protein, S cerevisiaeTrans-ActivatorsTranscription FactorsYDJ1 protein, S cerevisiae

Identifiers

PMID11689685
PMCPMC99961
OpenAlexW2140672160

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.