Purification, crystallization and X-ray diffraction analysis of the DNA-binding domain of human heat-shock factor 2.

ABSTRACT: Cells respond to various proteotoxic stimuli and maintain protein homeostasis through a conserved mechanism called the heat-shock response, which is characterized by the enhanced synthesis of heat-shock proteins. This response is mediated by heat-shock factors (HSFs). Four genes encoding HSF1-HSF4 exist in the genome of mammals. In this protein family, HSF1 is the orthologue of the single HSF in lower eukaryotic organisms and is the major regulator of the heat-shock response, while HSF2, which shows low sequence homology to HSF1, serves as a developmental regulator. Increasing evidence has revealed biochemical properties and functional roles that are unique to HSF2, such as its DNA-binding preference and sumoylation patterns, which are distinct from those of HSF1. The structural basis for

SUBMITTER: Feng H 

PROVIDER: S-EPMC4822986 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature