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

DOI:
10.3791/60172-v

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00:08 min

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September 02, 2019

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, ,
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

Chapters

  • 00:04Title
  • 01:00HeLa Cell Preparation
  • 02:34S. cerevisiae Cell Preparation
  • 04:53Proximity Ligation Assay
  • 06:56Results: Transiently Formed Molecular Chaperone Assemblies Captured by PLA in Prokaryotic and Eukaryotic Cells
  • 08:26Conclusion

Summary

Automatic Translation

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

Keywords: In Situ MonitoringTransient Protein InteractionsChaperone ComplexesProteostasisProkaryotic And Eukaryotic CellsMicrobial InfectionsProtein AssembliesImmunohistochemistryImmunofluorescenceELISAImmunoprecipitationsPoly-L-LysineParaformaldehydeTriton-X100S. Cerevisiae

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