Structural highlights
Function
HSF2_HUMAN DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
Publication Abstract from PubMed
Heat-shock transcription factor (HSF) family members function in stress protection and in human diseases including proteopathies, neurodegeneration and cancer. The mechanisms that drive distinct post-translational modifications, cofactor recruitment and target-gene activation for specific HSF paralogs are unknown. We present crystal structures of the human HSF2 DNA-binding domain (DBD) bound to DNA, revealing an unprecedented view of HSFs that provides insights into their unique biology. The HSF2 DBD structures resolve a new C-terminal helix that directs wrapping of the coiled-coil domain around DNA, thereby exposing paralog-specific sequences of the DBD surface for differential post-translational modifications and cofactor interactions. We further demonstrate a direct interaction between HSF1 and HSF2 through their coiled-coil domains. Together, these features provide a new model for HSF structure as the basis for differential and combinatorial regulation, which influences the transcriptional response to cellular stress.
Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors.,Jaeger AM, Pemble CW 4th, Sistonen L, Thiele DJ Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3150. PMID:26727490[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jaeger AM, Pemble CW 4th, Sistonen L, Thiele DJ. Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors. Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3150. PMID:26727490 doi:http://dx.doi.org/10.1038/nsmb.3150
