The C-terminal region of Drosophila heat shock factor (HSF) contains a constitutively functional transactivation domain.
The heat shock transcription factor (HSF) is constitutively expressed in Drosophila cells as an inactive monomer. Upon heat shock HSF undergoes trimerization and acquires high affinity DNA binding ability leading to specific interaction with its cognate elements in heat shock promoters. Here we show...
שמור ב:
| הוצא לאור ב: | Nucleic Acids Res |
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| Principais autores: | , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
Oxford University Press
1996
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC145630/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8628664/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/24.2.367 |
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