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Literature DB >> 26727489

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

Tobias Neudegger¹, Jacob Verghese¹, Manajit Hayer-Hartl¹, F Ulrich Hartl¹, Andreas Bracher¹.

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.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 2016 PMID： 26727489 DOI： 10.1038/nsmb.3149

Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369

75 in total

1. An efficient system for high-level expression and easy purification of authentic recombinant proteins.

Authors: Ann-Maree Catanzariti; Tatiana A Soboleva; David A Jans; Philip G Board; Rohan T Baker
Journal: Protein Sci Date: 2004-05 Impact factor: 6.725

2. A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1.

Authors: Daniel W Neef; Alex M Jaeger; Rocio Gomez-Pastor; Felix Willmund; Judith Frydman; Dennis J Thiele
Journal: Cell Rep Date: 2014-10-30 Impact factor: 9.423

3. A single amino acid can determine the DNA binding specificity of homeodomain proteins.

Authors: J Treisman; P Gönczy; M Vashishtha; E Harris; C Desplan
Journal: Cell Date: 1989-11-03 Impact factor: 41.582

4. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression.

Authors: K Abravaya; M P Myers; S P Murphy; R I Morimoto
Journal: Genes Dev Date: 1992-07 Impact factor: 11.361

5. In vitro activation of purified human heat shock factor by heat.

Authors: J S Larson; T J Schuetz; R E Kingston
Journal: Biochemistry Date: 1995-02-14 Impact factor: 3.162

6. How good are my data and what is the resolution?

Authors: Philip R Evans; Garib N Murshudov
Journal: Acta Crystallogr D Biol Crystallogr Date: 2013-06-13

Review 7. Dynamic remodeling of transcription complexes by molecular chaperones.

Authors: Richard I Morimoto
Journal: Cell Date: 2002-08-09 Impact factor: 66.850

8. In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress.

Authors: Caroline Jolly; Lara Konecny; Deborah L Grady; Yulia A Kutskova; Jose J Cotto; Richard I Morimoto; Claire Vourc'h
Journal: J Cell Biol Date: 2002-03-04 Impact factor: 10.539

9. HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers.

Authors: Marc L Mendillo; Sandro Santagata; Martina Koeva; George W Bell; Rong Hu; Rulla M Tamimi; Ernest Fraenkel; Tan A Ince; Luke Whitesell; Susan Lindquist
Journal: Cell Date: 2012-08-03 Impact factor: 41.582

10. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis.

Authors: Chengkai Dai; Luke Whitesell; Arlin B Rogers; Susan Lindquist
Journal: Cell Date: 2007-09-21 Impact factor: 41.582

38 in total

1. Molecular basis of HSF regulation.

Authors: Akira Nakai
Journal: Nat Struct Mol Biol Date: 2016-02 Impact factor: 15.369

Review 2. Tailoring of Proteostasis Networks with Heat Shock Factors.

Authors: Jenny Joutsen; Lea Sistonen
Journal: Cold Spring Harb Perspect Biol Date: 2019-04-01 Impact factor: 10.005

3. The synthesis of diapause-specific molecular chaperones in embryos of Artemia franciscana is determined by the quantity and location of heat shock factor 1 (Hsf1).

Authors: Jiabo Tan; Thomas H MacRae
Journal: Cell Stress Chaperones Date: 2019-01-30 Impact factor: 3.667

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

1. An efficient system for high-level expression and easy purification of authentic recombinant proteins.

2. A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1.

3. A single amino acid can determine the DNA binding specificity of homeodomain proteins.

4. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression.

5. In vitro activation of purified human heat shock factor by heat.

6. How good are my data and what is the resolution?

Review 7. Dynamic remodeling of transcription complexes by molecular chaperones.

8. In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress.

9. HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers.

10. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis.

1. Molecular basis of HSF regulation.

Review 2. Tailoring of Proteostasis Networks with Heat Shock Factors.

3. The synthesis of diapause-specific molecular chaperones in embryos of Artemia franciscana is determined by the quantity and location of heat shock factor 1 (Hsf1).

4. Rational design and screening of peptide-based inhibitors of heat shock factor 1 (HSF1).

5. RNA-seq Analysis Reveals Alternative Splicing Under Heat Stress in Rainbow Trout (Oncorhynchus mykiss).

6. Kinetic principles underlying pioneer function of GAGA transcription factor in live cells.

Review 7. The Multifaceted Role of HSF1 in Tumorigenesis.

Review 8. Regulation of heat shock transcription factors and their roles in physiology and disease.

9. A novel missense mutation in HSF4 causes autosomal-dominant congenital lamellar cataract in a British family.

10. The pericentromeric protein shugoshin 2 cooperates with HSF1 in heat shock response and RNA Pol II recruitment.