In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human CellsNiels Alberts *1, Yasith Mathangasinghe *2, Nadinath B. Nillegoda 3
1Department of Biomedical Sciences of Cells & Systems, University of Groningen, 2Department of Anatomy, Faculty of Medicine, University of Colombo, 3Australian Regenerative Medicine Institute (ARMI), Monash University
Cognate J-domain proteins cooperate with the Hsp70 chaperone to assist in a myriad of biological processes ranging from protein folding to degradation. Here, we describe an in situ proximity ligation assay, which allows the monitoring of these transiently formed chaperone machineries in bacterial, yeast and human cells.
