ArticleMolecular and cellular biology2003
Structural environment dictates the biological significance of heme-responsive motifs and the role of Hsp90 in the activation of the heme activator protein Hap1.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 36 citations in OpenAlex.
- Regulation of heme utilization and homeostasis in Candida albicans.PLoS genetics · 2022Article
- "Labile" heme critically regulates mitochondrial biogenesis through the transcriptional co-activator Hap4p inThe Journal of biological chemistry · 2020Article
- Heme promotes transcriptional and demethylase activities of Gis1, a member of the histone demethylase JMJD2/KDM4 family.Nucleic acids research · 2018Article
- A review on hemeoxygenase-2: focus on cellular protection and oxygen response.Oxidative medicine and cellular longevity · 2014Review
- Thiol/Disulfide redox switches in the regulation of heme binding to proteins.Antioxidants & redox signaling · 2011Review
- Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state.The Journal of biological chemistry · 2009Article
- The structural basis of gas-responsive transcription by the human nuclear hormone receptor REV-ERBbeta.PLoS biology · 2009Article
- Regulation of the HAP1 gene involves positive actions of histone deacetylases.Biochemical and biophysical research communications · 2007Article
- Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding.The Journal of biological chemistry · 2007Article
- Dynamical remodeling of the transcriptome during short-term anaerobiosis in Saccharomyces cerevisiae: differential response and role of Msn2 and/or Msn4 and other factors in galactose and glucose media.Molecular and cellular biology · 2005Article
- The heme activator protein Hap1 represses transcription by a heme-independent mechanism in Saccharomyces cerevisiae.Genetics · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Heme-responsive motifs (HRMs) mediate heme regulation of diverse regulatory proteins. The heme activator protein Hap1 contains seven HRMs, but only one of them, HRM7, is essential for heme activation of Hap1. To better understand the molecular basis underlying the biological significance of HRMs, we examined the effects of various mutations of HRM7 on Hap1. We found that diverse mutations of HRM7 significantly diminished the extent of Hap1 activation by heme and moderately enhanced the interaction of Hap1 with Hsp90. Furthermore, deletions of nonregulatory sequences completely abolished heme activation of Hap1 and greatly enhanced the interaction of Hap1 with Hsp90. These results show that the biological functions of HRMs and Hsp90 are highly sensitive to structural changes. The unique role of HRM7 in heme activation stems from its specific structural environment, not its mere presence. Likewise, the role of Hsp90 in Hap1 activation is dictated by the conformational or structural state of Hap1, not by the mere strength of Hap1-Hsp90 interaction. It appears likely that HRM7 and Hsp90 act together to promote the Hap1 conformational changes that are necessary for Hap1 activation. Such fundamental mechanisms of HRM-Hsp90 cooperation may operate in diverse regulatory systems to mediate signal transduction.
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