Related Experiment Video
Updated: Jun 22, 2026

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks
Published on: November 10, 2016
Alpha-helix 1 in the DNA-binding domain of heat shock factor 1 regulates its heat-induced trimerization and
Ming Lu1, Kwang-Jea Sohn, Si-Won Kim
1Department of Chemistry, Pusan National University, Busan 609-735, Republic of Korea.
Abstract:
Heat shock factor 1 (HSF1) primarily regulates various cellular stress responses. The role of alpha-helix1 (H1) in its DNA-binding domain (DBD) during HSF1 activation remains unknown. Here, HSF1 lacking H1 loses its heat-induced activity, suggesting the importance of the latter. Furthermore, the CD spectra and AMBER prediction show that this H1 deficiency does not change the structure of HSF1 monomer, but does impact its heat-induced trimerization. Point mutation showed that Phe18 in H1 interacts with Tyr60, and that Trp23 interacts with Phe104 by an aromatic-aromatic interaction. Thus, the presence of H1 stabilizes the DBD structure, which facilitates the heat-induced trimerization and DNA-binding of HSF1.
Related Concept Videos
Single-Strand DNA Binding Proteins
DNA Helicases
Molecular Chaperones and Protein Folding
The...
Diversity of Archaea IV
Diversity of Archaea III
Bacterial Protein Maturation

