Distinct quaternary structures of the AAA+ Lon protease control substrate degradation
Name
Vieux-2013-Distinct quaternary.pdf
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3.9 MB
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Author(s)
Vieux (Kloss), Ellen
Wohlever, Matthew Lee
Chen, James Z.
Baker, Tania
Sauer, Robert T
Date Issued
May 2013
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
Vieux, E. F., M. L. Wohlever, J. Z. Chen, R. T. Sauer, and T. A. Baker. “Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.” Proceedings of the National Academy of Sciences 110, no. 22 (May 28, 2013): E2002-E2008.
Version
Final published version
Abstract
Lon is an ATPase associated with cellular activities (AAA+) protease that controls cell division in response to stress and also degrades misfolded and damaged proteins. Subunits of Lon are known to assemble into ring-shaped homohexamers that enclose an internal degradation chamber. Here, we demonstrate that hexamers of Escherichia coli Lon also interact to form a dodecamer at physiological protein concentrations. Electron microscopy of this dodecamer reveals a prolate structure with the protease chambers at the distal ends and a matrix of N domains forming an equatorial hexamer–hexamer interface, with portals of ∼45 Å providing access to the enzyme lumen. Compared with hexamers, Lon dodecamers are much less active in degrading large substrates but equally active in degrading small substrates. Our results support a unique gating mechanism that allows the repertoire of Lon substrates to be tuned by its assembly state.
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/10.1073/pnas.1307066110
