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Article

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

Molecular microbiology - 1 Jan 2014

Wohlever Matthew L, Baker Tania A, Sauer Robert T

Abstract excerpt

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...

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Share to Adenosine Triphosphatases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 24205897
DOI: 10.1111/mmi.12444
PMCID: PMC3877180

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.PMID 24205897Read ↗

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