Abstract
The Hsp40/Hsp70 chaperone families combine a versatile folding capacitywith high specificity, which is mainly facilitated by Hsp40s. The structureand function of many Hsp40s remain poorly understood, particularly for theoligomeric Hsp40s that have a potent ability to suppress aggregation bypolyglutamine and other proteins. Here, our combined in vitro, in vivo, andin silico studies shed new light on the architecture, assembly and domaininteractions of Hsp40 protein, DnaJB8, and how it regulates recruitment ofpartner Hsp70s.
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