Evidence map›Paper›PMID 9632766›Full record

ArticleMolecular and cellular biology1998

Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1.

L Zhang, A Hach, C Wang

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Review
  3. Proteomic analysis of haem-binding protein fromPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Hypoxia elicits broad and systematic changes in protein subcellular localization.American journal of physiology. Cell physiology · 2011
    Article
  12. Nitric oxide and nitrosative stress tolerance in yeast.Biochemical Society transactions · 2011
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Regulation of the HAP1 gene involves positive actions of histone deacetylases.Biochemical and biophysical research communications · 2007
    Article
  18. 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
  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

3 authors at 1 institution in 1 country.

L ZhangDepartment of Biochemistry, NYU Medical Center, New York, New York 10016, USA. zhang102@mcrcr.med.nyu.edu
A Hach
C Wang
NYU Langone Health · US

Funding

MECHANISMS OF HEME SIGNALING IN EUKARYOTIC CELLSR01GM053453 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ZHANG, LI · 1997 to 2001
$477k
NIGMS NIH HHS GM53453
6 · The paper itself

Abstract

Apart from serving as a prosthetic group in globins and enzymes, heme is a key regulator controlling a wide range of molecular and cellular processes involved in oxygen sensing and utilization. To gain insights into molecular mechanisms of heme signaling and oxygen sensing in eukaryotes, we investigated the yeast heme-responsive transcriptional activator HAP1. HAP1 activity is regulated precisely and tightly by heme. Here we show that in the absence of heme, HAP1 forms a biochemically distinctive higher-order complex. Our data suggest that this complex contains HAP1 and four other cellular proteins including Hsp82 and Ydj1. The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity. Further, we determined HAP1 domains required for heme regulation: three domains-the dimerization domain, the heme domain, and the HRM7 (heme-responsive motif 7) domain-cooperate to form the higher-order complex and mediate heme regulation. Strikingly, we uncovered a novel function for the HAP1 dimerization domain: it not only allows dimerization but also provides critical functions in heme regulation and transcriptional activation. Our studies provide significant insights into the molecular events leading to heme activation of HAP1 and may shed light on molecular mechanisms of various heme-controlled biological processes in diverse organisms.

Indexed as

Carbon-Oxygen LyasesDNA-(Apurinic or Apyrimidinic Site) LyaseSignal TransductionAnimalsBinding SitesDimerizationFungal ProteinsHeat-Shock ProteinsHemeHSP40 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsNuclear ProteinsRabbitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional ActivationCarbon-Oxygen LyasesDNA-(Apurinic or Apyrimidinic Site) LyaseFungal ProteinsHeat-Shock ProteinsHemeHSP40 Heat-Shock ProteinsHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsYDJ1 protein, S cerevisiae

Identifiers

PMID9632766
PMCPMC108966
OpenAlexW2154828593

What OpenQuestion holds

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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.