The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.

ABSTRACT: Hsp70 is a highly conserved chaperone that in addition to providing essential cellular functions and aiding in cell survival following exposure to a variety of stresses is also a key modulator of prion propagation. Hsp70 is composed of a nucleotide-binding domain (NBD) and substrate-binding domain (SBD). The key functions of Hsp70 are tightly regulated through an allosteric communication network that coordinates ATPase activity with substrate-binding activity. How Hsp70 conformational changes relate to functional change that results in heat shock and prion-related phenotypes is poorly understood. Here, we utilised the yeast [PSI ⁺] system, coupled with SBD-targeted mutagenesis, to investigate how allosteric changes within key structural regions of the Hsp70 SBD result in functio

SUBMITTER: Xu L 

PROVIDER: S-EPMC5852193 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature