Single-molecule FRET probes allosteric effects on protein-translocating pore loops of a AAA+ machine.

ABSTRACT: AAA+ proteins (ATPases associated with various cellular activities) comprise a family of powerful ring-shaped ATP-dependent translocases that carry out numerous vital substrate-remodeling functions. ClpB is a AAA+ protein disaggregation machine that forms a two-tiered hexameric ring, with flexible pore loops protruding into its center and binding to substrate proteins. It remains unknown whether these pore loops contribute only passively to substrate-protein threading or have a more active role. Recently, we have applied single-molecule FRET spectroscopy to directly measure the dynamics of substrate-binding pore loops in ClpB. We have reported that the three pore loops of ClpB (PL1-3) undergo large-scale fluctuations on the microsecond timescale that are likely to be mechanistically import

SUBMITTER: Iljina M 

PROVIDER: S-EPMC10870172 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature