Results: Transiently Formed Molecular Chaperone Assemblies Captured by PLA in Prokaryotic and Eukaryotic Cells
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This method captures transient protein interactions in organisms like bacteria and yeast and in different cell types. Here we monitor transiently formed specific chaperone complexes that are involved in cellular proteostasis. The main advantage of
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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.