Mechanochemical basis of protein degradation by a double-ring AAA+ machine
Name
Baker_Mechanochemical basis.pdf
Size
1.19 MB
Format
Adobe PDF
Checksum (MD5)
5f2e41ea663e1c308123993ed78ea3f9
Author(s)
Iosefson, Ohad
Olivares, Adrian O.
Baker, Tania
Nager, Andrew Ross
Sauer, Robert T
Date Issued
September 2014
Journal
Nature Structural & Molecular Biology
Publisher
Nature Publishing Group
Citation
Olivares, Adrian O, Andrew R Nager, Ohad Iosefson, Robert T Sauer, and Tania A Baker. “Mechanochemical Basis of Protein Degradation by a Double-Ring AAA+ Machine.” Nature Structural & Molecular Biology 21, no. 10 (September 7, 2014): 871–875.
Version
Author's final manuscript
Abstract
Molecular machines containing double or single AAA+ rings power energy-dependent protein degradation and other critical cellular processes, including disaggregation and remodeling of macromolecular complexes. How the mechanical activities of double-ring and single-ring AAA+ enzymes differ is unknown. Using single-molecule optical trapping, we determine how the double-ring ClpA enzyme from Escherichia coli, in complex with the ClpP peptidase, mechanically degrades proteins. We demonstrate that ClpA unfolds some protein substrates substantially faster than does the single-ring ClpX enzyme, which also degrades substrates in collaboration with ClpP. We find that ClpA is a slower polypeptide translocase and that it moves in physical steps that are smaller and more regular than steps taken by ClpX. These direct measurements of protein unfolding and translocation define the core mechanochemical behavior of a double-ring AAA+ machine and provide insight into the degradation of proteins that unfold via metastable intermediates.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1038/nsmb.2885
