Chaperones substrate conformation

Another structural feature that may facilitate the retrotranslocation of RTA is its inherent ability to adopt metastable conformations in solution (McHugh et al., 2004). In this model, a significant fraction of RTA would transiently adopt a partly unfolded state in which the hydrophobic surfaces of the RTA C-terminal domain are exposed to the ERAD mechanism on dissociation of RTB. The N-terminal domain of RTA, which is more stable in solution than is RTA (Olson et al., 2004), would provide a structural anchor for refolding RTA to the functional 7V-glycosidase conformation, perhaps with the aid of appropriate chaperones. Potential chaperones for refolding in the cytosol include host cell proteins or the rRNA substrate itself (Argent et al., 2000). 

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