Ontology highlight
ABSTRACT:
SUBMITTER: Kotamarthi HC
PROVIDER: S-EPMC7888974 | biostudies-literature | 2020 Feb
REPOSITORIES: biostudies-literature
Kotamarthi Hema Chandra HC Sauer Robert T RT Baker Tania A TA
Cell reports 20200201 8
ATP-powered unfoldases containing D1 and D2 AAA+ rings play important roles in protein homeostasis, but uncertainty about the function of each ring remains. Here we use single-molecule optical tweezers to assay mechanical unfolding and translocation by a variant of the ClpAP protease containing an ATPase-inactive D1 ring. This variant displays substantial mechanical defects in both unfolding and translocation of protein substrates. Notably, when D1 is hydrolytically inactive, ClpAP often stalls ...[more]