Related Experiment Video
Updated: Aug 15, 2026

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
Published on: July 9, 2013
Proteolytic mapping of heat shock transcription factor domains
1Laboratory of Biochemistry, National Cancer Institute, Bethesda, Maryland 20892-4255, USA.
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.
More Related Videos
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Molecular Chaperones and Protein Folding
The...
Eukaryotic Transcription Activators
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These domains are...
Conservation of Protein Domains
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
General Transcription Factors

