ArticleProtein science : a publication of the Protein Society1996
Proteolytic mapping of heat shock transcription factor domains.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- The Torso signaling pathway modulates a dual transcriptional switch to regulate tailless expression.Nucleic acids research · 2009Article
- Complex regulation of the yeast heat shock transcription factor.Molecular biology of the cell · 2000Article
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Authors and funding
2 authors.
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Abstract
Heat shock transcription factors (HSFs) of higher eukaryotes respond to physical and cellular stress signals by trimerizing, binding to a specific site on DNA, and transactivating genes encoding the heat shock proteins. In this work, limited proteolysis was used as a biochemical probe of the domain organization of Drosophila HSF. Both unshocked monomeric and heat-shocked trimeric HSF possess an internal protease-sensitive region located between the amino-terminal and carboxyl-terminal hydrophobic heatad repeats, suggesting that this is a less structured region compared to those defined for DNA-binding, trimerization, and transactivation. For a few cleavage sites, the heat-shocked form of HSF is more accessible to proteases than the unshocked form, providing an additional diagnostic marker for inducible changes in conformation or modification between the latent and activated forms of HSF.
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