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  Structure of human heat-shock transcription factor 1 in complex with DNA

Neudegger, T., Verghese, J., Hayer-Hartl, M., Hartl, F. U., & Bracher, A. (2016). Structure of human heat-shock transcription factor 1 in complex with DNA. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 23(2), 140-146. doi:10.1038/nsmb.3149.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C802-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C803-B
Genre: Journal Article

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 Creators:
Neudegger, Tobias1, Author              
Verghese, Jacob1, Author              
Hayer-Hartl, Manajit2, Author              
Hartl, F. Ulrich1, Author              
Bracher, Andreas1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: COILED-COIL; MOLECULAR CHAPERONES; THERAPEUTIC TARGET; PROTEIN STRUCTURES; BINDING ACTIVITY; GENE-EXPRESSION; STRESS-RESPONSE; KEY FEATURES; FACTOR HSF1; FACTOR-I
 Abstract: Heat-shock transcription factor 1 (HSF1) has a central role in mediating the protective response to protein conformational stresses in eukaryotes. HSF1 consists of an N-terminal DNA-binding domain (DBD), a coiled-coil oligomerization domain, a regulatory domain and a transactivation domain. Upon stress, HSF1 trimerizes via its coiled-coil domain and binds to the promoters of heat shock protein-encoding genes. Here, we present cocrystal structures of the human HSF1 DBD in complex with cognate DNA. A comparative analysis of the HSF1 paralog Skn7 from Chaetomium thermophilum showed that single amino acid changes in the DBD can switch DNA binding specificity, thus revealing the structural basis for the interaction of HSF1 with cognate DNA. We used a crystal structure of the coiled-coil domain of C. thermophilum Skn7 to develop a model of the active human HSF1 trimer in which HSF1 embraces the heat-shock-element DNA.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000369220800010
DOI: 10.1038/nsmb.3149
 Degree: -

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Title: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 23 (2) Sequence Number: - Start / End Page: 140 - 146 Identifier: ISSN: 1545-9993