Pre-N and C-terminal extension regions of Arabidopsis HSP90.7 regulate the chaperone activity and ER stress response.

ABSTRACT: The endoplasmic reticulum (ER)-localized molecular chaperone heat shock protein 90.7 (HSP90.7) plays a critical role in maintaining protein homeostasis in plants, particularly under stress conditions. However, the functional roles of its pre-N-terminal region (pre-N) and C-terminal extension (CTE) regions remain poorly understood. In this study, we integrated molecular dynamics simulations, in vitro biochemical assays, and in vivo mutant analysis to investigate the roles of these regions. Deletion of either region did not affect normal seedling development but conferred pronounced hypersensitivity to ER stress. Molecular dynamics simulations revealed that both the pre-N and CTE form regulatory contacts with HSP90.7's N-terminal, middle, and C-terminal domains, likely modulating the chapero

SUBMITTER: Noureddine J 

PROVIDER: S-EPMC12639838 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature