ArticleMolecular microbiology2014
Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lipid bilayer properties govern substrate engagement and extraction by the AAA+ ATPase Msp1.The Journal of biological chemistry · 2025Article
- Overcoming fluorescence loss in mEOS-based AAA+ unfoldase reporters through covalent linkage.Protein expression and purification · 2025Article
- Global impacts of peroxisome and pexophagy dysfunction revealed through multi-omics analyses of lon2 and atg2 mutants.The Plant journal : for cell and molecular biology · 2024Article
- The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024Article
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Transcriptomic characterization of Lonrf1 at the single-cell level under pathophysiological conditions.Journal of biochemistry · 2023Article
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Plant peroxisome proteostasis-establishing, renovating, and dismantling the peroxisomal proteome.Essays in biochemistry · 2022Review
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- The first case report of CODAS syndrome in Chinese population caused by twoFrontiers in genetics · 2022Article
- Enhancing protein perdeuteration by experimental evolution of Escherichia coli K-12 for rapid growth in deuterium-based media.Protein science : a publication of the Protein Society · 2021Article
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
- Article
- Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.Science advances · 2020Article
- Sorting out how Msp1 maintains mitochondrial membrane proteostasis.Mitochondrion · 2019Review
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
- New insights into structural and functional relationships between LonA proteases and ClpB chaperones.FEBS open bio · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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.
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