Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity
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Author(s)
Baker, Tania
Wohlever, Matthew Lee
Sauer, Robert T
Date Issued
November 2013
Journal
Molecular Microbiology
Publisher
Wiley Blackwell
Citation
Wohlever, Matthew L., Tania A. Baker, and Robert T. Sauer. “Roles of the N Domain of the AAA+ Lon Protease in Substrate Recognition, Allosteric Regulation and Chaperone Activity.” Molecular Microbiology 91, no. 1 (November 10, 2013): 66–78.
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Author's final manuscript
Abstract
Degron binding regulates the activities of the AAA+ Lon protease in addition to targeting proteins for degradation. The sul20 degron from the cell-division inhibitor SulA is shown here to bind to the N domain of Escherichia coli Lon, and the recognition site is identified by cross-linking and scanning for mutations that prevent sul20-peptide binding. These N-domain mutations limit the rates of proteolysis of model sul20-tagged substrates and ATP hydrolysis by an allosteric mechanism. Lon inactivation of SulA in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber. Lon-mediated relief of proteotoxic stress and protein aggregation in vivo can also occur without degradation but is not dependent on robust ATP hydrolysis. In combination, these results demonstrate that Lon can function as a protease or a chaperone and reveal that some of its ATP-dependent biological activities do not require translocation.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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DOI of Published Version
https://doi.org/10.1111/mmi.12444
