The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.

ABSTRACT: The small heat shock protein (sHsp) chaperones are crucial for cell survival and can prevent aggregation of client proteins that partially unfold under destabilizing conditions. Most investigations on the chaperone activity of sHsps are based on a limited set of thermosensitive model substrate client proteins since the endogenous targets are often not known. There is a high diversity among sHsps with a single conserved β-sandwich fold domain defining the family, the α-crystallin domain, whereas the N-terminal and C-terminal regions are highly variable in length and sequence among various sHsps and conserved only within orthologues. The endogenous targets are probably also varying among various sHsps, cellular compartments, cell type and organism. Here we have investigated Hsp21, a non-meta

SUBMITTER: Bernfur K 

PROVIDER: S-EPMC5563132 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature