Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines
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NRMicro_Sauer_MS_RTS_10_16[1].pdf
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Author(s)
Olivares, Adrian O.
Baker, Tania
Sauer, Robert T.
Date Issued
December 2015
Journal
Nature Reviews Microbiology
Publisher
Nature Publishing Group
Citation
Olivares, Adrian O., Tania A. Baker, and Robert T. Sauer. “Mechanistic Insights into Bacterial AAA+ Proteases and Protein-Remodelling Machines.” Nature Reviews Microbiology 14, no. 1 (December 7, 2015): 33–44. ©2015 Nature Publishing Group
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Author's final manuscript
Abstract
To maintain protein homeostasis, AAA+ proteolytic machines degrade damaged and unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP-dependent unfolding of a target protein and its subsequent translocation into a self-compartmentalized proteolytic chamber. Related AAA+ enzymes also disaggregate and remodel proteins. Recent structural and biochemical studies, in combination with direct visualization of unfolding and translocation in single-molecule experiments, have illuminated the molecular mechanisms behind these processes and suggest how remodelling of macromolecular complexes by AAA+ enzymes could occur without global denaturation. In this Review, we discuss the structural and mechanistic features of AAA+ proteases and remodelling machines, focusing on the bacterial ClpXP and ClpX as paradigms. We also consider the potential of these enzymes as antibacterial targets and outline future challenges for the field.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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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.
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DOI of Published Version
https://doi.org/10.1038/nrmicro.2015.4
