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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
 

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Article DOI: 10.3791/60172-v • 08:58 min • September 2nd, 2019
September 2nd, 2019 •
*1, *2, 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
* These authors contributed equally

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résumé
Automatic Translation

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.

Tags

In Situ Monitoring Transient Protein Interactions Chaperone Complexes Cellular Proteostasis Dynamics Sub-cellular Localization Prokaryotic Cells Eukaryotic Cells Microbial Infections Sample Preparation Phase Antibodies Poly-L-Lysine Diagnostic Slides Cell Growth
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