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

被引：7
作者：
Ota, Azumi [1 ]
Enoki, Yasuald [1 ]
Yamamoto, Noritaka [1 ]
Sawai, Maki [1 ]
Sakurai, Hiroshi [1 ]
机构：
[1] Kanazawa Univ, Grad Sch Med Sci, Div Hlth Sci, Kanazawa, Ishikawa 9200942, Japan
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS | 2013年 / 1829卷 / 09期
关键词：
Heat shock transcription factor (HSF); Protein-DNA interaction; Intramolecular interaction; Oligomer formation; FACTOR FAMILY; FACTOR-I; HUMAN HSF1; STRESS; ACTIVATION; RECOGNITION; ADAPTATION; EXPRESSION; REPRESSION; COMPLEX;
D O I：
10.1016/j.bbagrm.2013.03.011
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.(c) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码：930 / 936
页数：7
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