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Heat shock-induced chaperoning by Hsp70 is enabled in-cell.

PLoS ONE. 2019; 
Guin Drishti,Gelman Hannah,Wang Yuhan,Gruebele Ma
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Custom Vector Construction 1/MCS vector by Genscript Corp.... Stopped flow PGK refolding assay To monitor PGK unfolding and refolding, a FRET-labeled PGK1 (FRET-PGK1) was designed with an N-terminal mEGFP and a C-terminal mCherry label and cloned into a pDream vector by Genscript [31]. Get A Quote

摘要

Recent work has shown that weak protein-protein interactions are susceptible to the cellular milieu. One case in point is the binding of heat shock proteins (Hsps) to substrate proteins in cells under stress. Upregulation of the Hsp70 chaperone machinery at elevated temperature was discovered in the 1960s, and more recent studies have shown that ATPase activity in one Hsp70 domain is essential for control of substrate binding by the other Hsp70 domain. Although there are several denaturant-based assays of Hsp70 activity, reports of ATP-dependent binding of Hsp70 to a globular protein substrate under heat shock are scarce. Here we show that binding of heat-inducible Hsp70 to phosphoglycerate kinase (PGK) is ... More

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