Recombinant Expression and Purification of the Cyanobacterial Chaperone HtpG from <i>Synechococcus elongatus</i> PCC 7942.

ABSTRACT: The 90 kDa Heat Shock Protein (Hsp90) is an essential and highly conserved molecular chaperone that supports the folding and maturation of a diverse array of client proteins across prokaryotic and eukaryotic organisms. In bacteria, HtpG, the Hsp90 homolog, plays a central role in stress response and protein homeostasis, particularly under high-temperature and other stress conditions. Despite extensive studies on HtpG from E. coli, the biochemical properties and functional roles of cyanobacterial HtpG remain poorly characterized. Here, we focus on HtpG from the cyanobacterium Synechococcus elongatus PCC 7942 (seHtpG), a model organism for photosynthesis and circadian rhythm research. We developed a method for the overexpression and purification of seHtpG in E. coli, ach

SUBMITTER: Jiang L 

PROVIDER: S-EPMC12452654 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature