Hsp72 chaperone function is dispensable for protection against stress-induced apoptosis.

摘要: In addition to its role as a molecular chaperone, heat shock protein 72 (Hsp72) protects cells against wide range of apoptosis inducing stresses. However, it is unclear if these two roles are functionally related or whether Hsp72 inhibits by mechanism independent chaperone activity. The N-terminal adenosine triphosphatase domain, substrate-binding domain and the C-terminal EEVD regulatory motif all essential for this study, we show that mutants with functional but lacking activity retain their ability protect induced tumor necrosis factor alpha. contrast, deletion mutant has no protective capacity. inhibit effects triphosphate-binding indicates inhibition may involve stable binding interaction substrate rather than