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. Copyright 2001 Academic Press.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|