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Biochem Biophys Res Commun. 2001 Jul 20;285(3):696-701.

A novel domain of the yeast heat shock factor that regulates its activation function.

Author information

1
School of Health Sciences, Faculty of Medicine, Kanazawa University, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan. sakurai@kenroku.kanazawa-u.ac.jp

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.

PMID:
11453649
DOI:
10.1006/bbrc.2001.5234
[Indexed for MEDLINE]

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