TorsinA is a member of the AAA+ ATPase family of proteins and, notably, is the only known
ATPase localized to the ER lumen. It has been suggested to act as a molecular chaperone,
while a mutant form associated with early-onset torsion dystonia, a dominantly inherited
movement disorder, appears to result in a net loss of function in vivo. Thus far, no studies
have examined the chaperone activity of torsinA in vitro. Here we expressed and purified
both wild-type (WT) and mutant torsinA fusion proteins in bacteria and examined their ability …