ArticleProtein science : a publication of the Protein Society2012
Protein unfolding and degradation by the AAA+ Lon protease.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Proteostasis-targeted antibacterial strategies.Journal of microbiology (Seoul, Korea) · 2026Review
- Systematic analysis of structural disorder in the minimal proteome ofMicrobiology spectrum · 2025Article
- 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
- FtsH degrades dihydrofolate reductase by recognizing a partially folded species.Protein science : a publication of the Protein Society · 2022Article
- Biomolecular mechanisms for signal differentiation.iScience · 2021Article
- Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.FEBS letters · 2021Article
- Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.Nature communications · 2021Article
- N domain of the Lon AAA+ protease controls assembly and substrate choice.Protein science : a publication of the Protein Society · 2019Article
- N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen.Scientific reports · 2017Article
- Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Identification of a Degradation Signal Sequence within Substrates of the Mitochondrial i-AAA Protease.Journal of molecular biology · 2017Article
- Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane.Nature communications · 2016Article
- A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.Structure (London, England : 1993) · 2016Article
- Spatial and temporal dynamics of the cardiac mitochondrial proteome.Expert review of proteomics · 2015Review
- Adaptor-mediated Lon proteolysis restricts Bacillus subtilis hyperflagellation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mechanochemical basis of protein degradation by a double-ring AAA+ machine.Nature structural & molecular biology · 2014Article
- Stress-induced remodeling of the bacterial proteome.Current biology : CB · 2014Review
- Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.Molecular microbiology · 2014Article
- Interaction between chaperone and protease functions of LON2, and autophagy during the functional transition of peroxisomes.Plant signaling & behavior · 2014Article
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3 authors.
Funding
Abstract
AAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. What determines the ability of different AAA+ enzymes to unfold and thus degrade different native protein substrates is currently uncertain. Here, we explore the ability of the E. coli Lon protease to unfold and degrade model protein substrates beginning at N-terminal, C-terminal, or internal degrons. Lon has historically been viewed as a weak unfoldase, but we demonstrate robust and processive unfolding/degradation of some substrates with very stable protein domains, including mDHFR and titin(I27) . For some native substrates, Lon is a more active unfoldase than related AAA+ proteases, including ClpXP and ClpAP. For other substrates, this relationship is reversed. Thus, unfolding activity does not appear to be an intrinsic enzymatic property. Instead, it depends on the specific protease and substrate, suggesting that evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.