Multiple DNAJ-stimulated cycles of HSP70 binding promote polypeptide folding, sometimes in cooperation with other chaperone systems (Palleros et al., 1993; Szabo et al., 1994; Mayer and Bukau, 2005; Kampinga and Craig, 2010; Young, 2010; Hartl et al., 2011).
Hsp70 chaperone systems are ubiquitous.
The aggregation-prone proteins are enriched for multiple chaperone interactions, thus high protein abundance is probably counterbalanced by molecular chaperones to allow soluble expression in vivo.
Importantly, the As- and P-sets are enriched for multiple chaperone interactions (Fig. 5C), indicating a high demand of chaperone assistance for proper folding of these proteins.
Disrupting the function of these chaperone systems can allow mutant CFTR to escape degradation.
To deal with this task, mitochondria possess dedicated chaperone systems to assist in these processes.
This finding is also likely to have general relevance to other amyloid and chaperone systems.
As such, their aggregation can be significantly recovered with the assistance of cellular chaperone systems.
Release and refolding of both complexes and aggregates need the cooperation of ATP-dependent chaperone systems.
We first investigated a combination of the two major chaperone systems with folding activity, KJE and ELS, and the co-operating chaperone with disaggregating activity, ClpB.
