BCL-2 athanogene 5 (BAG5), a molecular chaperone protein, contains 5 distinct BAG domains, each of which has the potential to bind with heat shock protein 70 (HSP70). BAG5 has been implicated in the progression of Parkinson's disease through inhibitory interactions with HSP70, parkin and CHIP, a U-box dependent E3 ubiquitin ligase. In order to study the effect of individual BAG domains on HSP70 and other proteins, full-length recombinant human BAG5 protein and truncated BAG domain segments have been produced in E. coli and purified using affinity and gel-filtration chromatography. Using in vitro refolding assays, the effect of BAG5 and the individual domains on HSP70 and HSP40-mediated refolding of client proteins has been determined.

Effect of individual domains from BCL-2 athanogene 5 (BAG5) on HSP70 activity

245th National Meeting (2013)

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