Equilibrium Binding of Wild-type and Mutant Drosophila Heat Shock Factor DNA Binding Domain with HSE DNA Studied by Analytical Ultracentrifugation

Bulletin of the Korean chemical society

Soon-Jong Kim¹  Jin-Ku Park¹ 

关键词: Heat shock factor;    HSF:HSE interaction;    Thermodynamic parameters;    Analytical ultracentrifuge;    Multi-wavelength scan;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

We have investigated binding between wild-type and mutant Heat Shock Factor (HSF) DNA binding domains (DBDs) with 17-bp HSE containing a central 5`-NGAAN-3` element by equilibrium analytical ultracentrifugation using multi-wavelength technique. Our results indicate that R102 plays critical role in HSE recognition and the interactions are characterized by substantial negative changes of enthalpy ( = −9.90 ± 1.13 kcal mol−1) and entropy ( = −12.46 ± 3.77 cal mol−1K−1) with free energy change, of −6.15 ± 0.03 kcal mol−1. N105 plays minor role in the HSE interactions with of −2.54 ± 1.65 kcal mol−1, of 19.28 ± 5.50 cal mol−1K−1 and of −8.35 ± 0.05 kcal mol−1, which are similar to those observed for wild-type DBD:HSE interactions ( = −3.31 ± 1.86 kcal mol−1, = 17.38 ± 6.20 cal mol−1K−1 and = −8.55 ± 0.06 kcal mol−1) indicating higher entropy contribution for both wild-type and N105A DBD bindings to the HSE.

【 授权许可】

Unknown