Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines.

ABSTRACT: AAA+ proteases and remodeling machines couple hydrolysis of ATP to mechanical unfolding and translocation of proteins following recognition of sequence tags called degrons. Here, we use single-molecule optical trapping to determine the mechanochemistry of two AAA+ proteases, Escherichia coli ClpXP and ClpAP, as they unfold and translocate substrates containing multiple copies of the titin^I27 domain during degradation initiated from the N terminus. Previous studies characterized degradation of related substrates with C-terminal degrons. We find that ClpXP and ClpAP unfold the wild-type titin^I27 domain and a destabilized variant far more rapidly when pulling from the N terminus, whereas translocation speed is reduced only modestly in the N-to-C direction. These m

SUBMITTER: Olivares AO 

PROVIDER: S-EPMC5547649 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature