DOI: 10.1111/mmi.12444. Roles of the <scp>N</scp> domain of the <scp>AAA</scp>+ <scp>Lon</scp> protease in substrate recognition, allosteric regulation and chaperone activity

Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity

10.1111/mmi.12444

Crossref journal-article

Wiley

Molecular Microbiology (311)

Abstract

SummaryDegron 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.

Bibliography

Wohlever, M. L., Baker, T. A., & Sauer, R. T. (2013). Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity. Molecular Microbiology, 91(1), 66â78. Portico.

Authors 3

Matthew L. Wohlever (first)
Tania A. Baker (additional)
Robert T. Sauer (additional)

References 50 Referenced 41

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Dates

Type	When
Created	11 years, 9 months ago (Oct. 29, 2013, 10:46 a.m.)
Deposited	1 year, 10 months ago (Oct. 2, 2023, 4:16 p.m.)
Indexed	4 months, 3 weeks ago (April 5, 2025, 4:46 a.m.)
Issued	11 years, 9 months ago (Nov. 10, 2013)
Published	11 years, 9 months ago (Nov. 10, 2013)
Published Online	11 years, 9 months ago (Nov. 10, 2013)
Published Print	11 years, 7 months ago (Jan. 1, 2014)

Funders 0

None

BibTeX

@article{Wohlever_2013, title={Roles of the <scp>N</scp> domain of the <scp>AAA</scp>+ <scp>Lon</scp> protease in substrate recognition, allosteric regulation and chaperone activity}, volume={91}, ISSN={1365-2958}, url={http://dx.doi.org/10.1111/mmi.12444}, DOI={10.1111/mmi.12444}, number={1}, journal={Molecular Microbiology}, publisher={Wiley}, author={Wohlever, Matthew L. and Baker, Tania A. and Sauer, Robert T.}, year={2013}, month=nov, pages={66–78} }

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