Marcin Jelen, Igor Grochowina, Aneta Grabinska-Rogala, Szymon J Ciesielski, Katarzyna Dabrowska, Bartlomiej Tomiczek, Lukasz Nierzwicki, Wojciech Delewski, Brenda Schilke, Jacek Czub, Michal Dadlez, Rafal Dutkiewicz, Elizabeth A Craig, Jaroslaw Marszalek
Hsp70 are ubiquitous, versatile molecular chaperones that cyclically interact with substrate protein(s). The initial step requires synergistic interaction of a substrate and a J-domain protein (JDP) cochaperone, via its J-domain, with Hsp70 to stimulate hydrolysis of its bound ATP. This hydrolysis drives conformational changes in Hsp70 that stabilize substrate binding. However, because of the transient nature of substrate and JDP interactions, this key step is not well understood. Here we leverage a well characterized Hsp70 system specialized for iron-sulfur cluster biogenesis, which like many systems, has a JDP that binds substrate on its own...
September 18, 2023: Journal of Molecular Biology