Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine.

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ID: 67156
2019
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Abstract
Large protein machines are tightly regulated through allosteric communication channels. Here we demonstrate the involvement of ultrafast conformational dynamics in allosteric regulation of ClpB, a hexameric AAA+ machine that rescues aggregated proteins. Each subunit of ClpB contains a unique coiled-coil structure, the middle domain (M domain), proposed as a control element that binds the co-chaperone DnaK. Using single-molecule FRET spectroscopy, we probe the M domain during the chaperone cycle and find it to jump on the microsecond time scale between two states, whose structures are determined. The M-domain jumps are much faster than the overall activity of ClpB, making it an effectively continuous, tunable switch. Indeed, a series of allosteric interactions are found to modulate the dynamics, including binding of nucleotides, DnaK and protein substrates. This mode of dynamic control enables fast cellular adaptation and may be a general mechanism for the regulation of cellular machineries.
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mazal2019tunablenature Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Hisham Mazal, Marija Iljina, Yoav Barak, Nadav Elad, Rina Rosenzweig, Pierre Goloubinoff, Inbal Riven, Gilad Haran
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Journal Nature communications
Year 2019
DOI
10.1038/s41467-019-09474-6
URL
Keywords
protein translocation hsp110 hsp70 disaggregation j cochaperones brownian ratchet chaperones entropic pulling motor proteins power-stroke

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