Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.

ABSTRACT: Cellular function depends on the correct folding of proteins inside the cell. Heat-shock proteins 70 (Hsp70s), being among the first molecular chaperones binding to nascently translated proteins, aid in protein folding and transport. They undergo large, coordinated intra- and interdomain structural rearrangements mediated by allosteric interactions. Here, we applied a three-color single-molecule Förster resonance energy transfer (FRET) combined with three-color photon distribution analysis to compare the conformational cycle of the Hsp70 chaperones DnaK, Ssc1, and BiP. By capturing three distances simultaneously, we can identify coordinated structural changes during the functional cycle. Besides the known conformations of the Hsp70s with docked domains and open lid and undocked domains wit

SUBMITTER: Voith von Voithenberg L 

PROVIDER: S-EPMC8379981 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature