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A novel domain of the yeast heat shock factor that regulates its activation function.
Biochem Biophys Res Commun. 2001 Jul 20; 285(3):696-701.BB

Abstract

Heat shock factor Hsf1 of the yeast Saccharomyces cerevisiae binds to the heat shock element (HSE) of a subset of genes and activates their transcription in response to various environmental stresses. Hsf1 protein contains discrete domains respectively involved in DNA-binding, trimerization, transcription activation, and transcription repression. Here we have identified a novel domain rich in basic amino acids at the extreme C-terminus of Hsf1. Deletion or point mutations of the C-terminal basic region caused an inefficient heat shock response of genes containing noncanonical HSEs such as CUP1 and HSP26. The basic region is also essential for oxidative stress-inducible transcription of CUP1 by Hsf1. By contrast, it was dispensable for heat induction through the canonical HSE. We suggest that the basic region is a modulator involved in regulation of the Hsf1-mediated activation depending on the architecture of its binding site.

Authors+Show Affiliations

School of Health Sciences, Faculty of Medicine, Kanazawa University, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan. sakurai@kenroku.kanazawa-u.ac.jpNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11453649

Citation

Sakurai, H, and T Fukasawa. "A Novel Domain of the Yeast Heat Shock Factor That Regulates Its Activation Function." Biochemical and Biophysical Research Communications, vol. 285, no. 3, 2001, pp. 696-701.
Sakurai H, Fukasawa T. A novel domain of the yeast heat shock factor that regulates its activation function. Biochem Biophys Res Commun. 2001;285(3):696-701.
Sakurai, H., & Fukasawa, T. (2001). A novel domain of the yeast heat shock factor that regulates its activation function. Biochemical and Biophysical Research Communications, 285(3), 696-701.
Sakurai H, Fukasawa T. A Novel Domain of the Yeast Heat Shock Factor That Regulates Its Activation Function. Biochem Biophys Res Commun. 2001 Jul 20;285(3):696-701. PubMed PMID: 11453649.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A novel domain of the yeast heat shock factor that regulates its activation function. AU - Sakurai,H, AU - Fukasawa,T, PY - 2001/7/17/pubmed PY - 2001/8/17/medline PY - 2001/7/17/entrez SP - 696 EP - 701 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 285 IS - 3 N2 - Heat shock factor Hsf1 of the yeast Saccharomyces cerevisiae binds to the heat shock element (HSE) of a subset of genes and activates their transcription in response to various environmental stresses. Hsf1 protein contains discrete domains respectively involved in DNA-binding, trimerization, transcription activation, and transcription repression. Here we have identified a novel domain rich in basic amino acids at the extreme C-terminus of Hsf1. Deletion or point mutations of the C-terminal basic region caused an inefficient heat shock response of genes containing noncanonical HSEs such as CUP1 and HSP26. The basic region is also essential for oxidative stress-inducible transcription of CUP1 by Hsf1. By contrast, it was dispensable for heat induction through the canonical HSE. We suggest that the basic region is a modulator involved in regulation of the Hsf1-mediated activation depending on the architecture of its binding site. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/11453649/A_novel_domain_of_the_yeast_heat_shock_factor_that_regulates_its_activation_function_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(01)95234-9 DB - PRIME DP - Unbound Medicine ER -