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In situ-monitorering af transitivt dannede molekylære Chaperone-samlinger i bakterier, gær og humane celler
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In situ-monitorering af transitivt dannede molekylære Chaperone-samlinger i bakterier, gær og humane celler

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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Cognate J-Domain proteiner samarbejder med Hsp70 chaperone for at hjælpe i et utal af biologiske processer, der spænder fra proteinfoldning til nedbrydning. Her beskriver vi en in situ nærheds ligationsanalyse, som tillader overvågning af disse transitivt dannede chaperone-maskiner i bakterie-, gær-og humane celler.

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Denne måned i JoVE nærhed ligation assay Chaperone J-Domain protein Hsp70 human bakterier gær E. coli S. cerevisiae protein interaktion proteostase
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