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Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone

Nat Commun. 2021-02; 
Bryan D Ryder, Irina Matlahov, Sofia Bali, Jaime Vaquer-Alicea, Patrick C A van der Wel, Lukasz A Joachimiak
Products/Services Used Details Operation
Custom DNA/RNA Oligos The primers used are listed in Supplementary Table 2. The DnaJB8F→S construct was purchased from Genscript Get A Quote

摘要

The Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificity, which is mainly facilitated by Hsp40s. The structure and function of many Hsp40s remain poorly understood, particularly oligomeric Hsp40s that suppress protein aggregation. Here, we used a combination of biochemical and structural approaches to shed light on the domain interactions of the Hsp40 DnaJB8, and how they may influence recruitment of partner Hsp70s. We identify an interaction between the J-Domain (JD) and C-terminal domain (CTD) of DnaJB8 that sequesters the JD surface, preventing Hsp70 interaction. We propose a model for DnaJB8-Hsp70 recruitment, whereby the JD-CTD interaction of DnaJB8 acts as a re... More

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