htpG
htpG is a bacterial gene encoding HtpG, the cytosolic member of the Hsp90 family of molecular chaperones. As an ATP-dependent chaperone, HtpG assists in the folding, stabilization, and reconfirmation of protein clients, particularly under stress conditions such as elevated temperatures. The protein typically functions as a homodimer and is composed of three domains: an N-terminal ATPase domain, a middle client-binding domain, and a C-terminal dimerization domain. Unlike many eukaryotic cytosolic Hsp90s, bacterial HtpG generally lacks the MEEVD motif found at the extreme C-terminus.
Expression of htpG is part of the bacterial heat shock response. In Escherichia coli and many other
Functionally, HtpG participates in maintaining proteostasis by assisting in the correct folding or stabilization of diverse
In research, htpG has served as a model for studying the interplay between Hsp90-family chaperones and other