Evolutionarily conserved domain of heat shock transcription factor negatively regulates oligomerization and DNA binding.
Identifieur interne : 000570 ( Ncbi/Merge ); précédent : 000569; suivant : 000571Evolutionarily conserved domain of heat shock transcription factor negatively regulates oligomerization and DNA binding.
Auteurs : Azumi Ota [Japon] ; Yasuaki Enoki ; Noritaka Yamamoto ; Maki Sawai ; Hiroshi SakuraiSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2013.
Descripteurs français
- KwdFr :
- ADN (métabolisme), Biopolymères (), Facteurs de transcription (), Facteurs de transcription (métabolisme), Facteurs de transcription (physiologie), Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (métabolisme), Protéines de liaison à l'ADN (physiologie), RT-PCR, Séquence conservée, Évolution biologique.
- MESH :
English descriptors
- KwdEn :
- Biological Evolution, Biopolymers (chemistry), Conserved Sequence, DNA (metabolism), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (metabolism), DNA-Binding Proteins (physiology), Heat Shock Transcription Factors, Reverse Transcriptase Polymerase Chain Reaction, Transcription Factors (chemistry), Transcription Factors (metabolism), Transcription Factors (physiology).
- MESH :
- chemical , chemistry : Biopolymers, DNA-Binding Proteins, Transcription Factors.
- chemical , metabolism : DNA, DNA-Binding Proteins, Transcription Factors.
- chemical , physiology : DNA-Binding Proteins, Transcription Factors.
- Biological Evolution, Conserved Sequence, Heat Shock Transcription Factors, Reverse Transcriptase Polymerase Chain Reaction.
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
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pubmed:23567048Le document en format XML
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<author><name sortKey="Yamamoto, Noritaka" sort="Yamamoto, Noritaka" uniqKey="Yamamoto N" first="Noritaka" last="Yamamoto">Noritaka Yamamoto</name>
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<term>DNA (metabolism)</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>DNA-Binding Proteins (physiology)</term>
<term>Heat Shock Transcription Factors</term>
<term>Reverse Transcriptase Polymerase Chain Reaction</term>
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<term>Facteurs de transcription ()</term>
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<term>Facteurs de transcription (physiologie)</term>
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<term>Facteurs de transcription</term>
<term>Protéines de liaison à l'ADN</term>
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<front><div type="abstract" xml:lang="en">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. </div>
</front>
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<Abstract><AbstractText>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. </AbstractText>
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