Serveur d'exploration Stress et Covid

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Evolutionarily conserved domain of heat shock transcription factor negatively regulates oligomerization and DNA binding.

Identifieur interne : 001082 ( Main/Exploration ); précédent : 001081; suivant : 001083

Evolutionarily conserved domain of heat shock transcription factor negatively regulates oligomerization and DNA binding.

Auteurs : Azumi Ota [Japon] ; Yasuaki Enoki ; Noritaka Yamamoto ; Maki Sawai ; Hiroshi Sakurai

Source :

RBID : pubmed:23567048

Descripteurs français

English descriptors

Abstract

Heat shock transcription factor (HSF) regulates the expression of genes encoding molecular chaperones and stress-responsive proteins. Conversion of HSF from a monomer to a homotrimer or heterotrimer is essential for its binding to heat shock elements (HSEs) comprised of inverted repeats of the pentamer nGAAn. Here, we constructed various human HSF1 derivatives and analyzed their transcriptional activity through the continuously and discontinuously arranged nGAAn units. We identified a short stretch of amino acids that inhibits the activation ability of HSF1, especially through discontinuous HSEs. This stretch is conserved in HSFs of various organisms, interacts with the hydrophobic repeat regions that mediate HSF oligomerization, and impedes homotrimer formation and DNA binding. This conserved domain plays an important role in maintaining HSF in an inactive monomeric form.

DOI: 10.1016/j.bbagrm.2013.03.011
PubMed: 23567048


Affiliations:


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