ArticleNature communications2023
The heat shock protein LarA activates the Lon protease in response to proteotoxic stress.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- A selective inhibitor reveals roles for LONP1 in mitochondrial proteostasis and OXPHOS dependencies.Life science alliance · 2026Article
- Structural Analysis of Human LonP1 Protease Bound with the Native Substrate.Life (Basel, Switzerland) · 2026Article
- Recognition of small Tim chaperones by the mitochondrial Yme1 protease.Protein science : a publication of the Protein Society · 2026Article
- Construction of probiotic Escherichia coli Nissle 1917 as a next-generation expression platform and its application in therapeutic protein production.Journal of biological engineering · 2025Article
- Mutations in the clpS Gene of Riemerella anatipestifer Affect Stress Response and Bacterial Virulence.Current microbiology · 2025Article
- 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
- Multigenerational proteolytic inactivation of restriction upon subtle genomic hypomethylation in Pseudomonas aeruginosa.Nature microbiology · 2025Article
- Structural basis for the allosteric activation of Lon by the heat shock protein LarA.Nature communications · 2025Article
- Chlorogenic acid inhibits virulence and resistance gene transfer in outer membrane vesicles of carbapenem-resistantFrontiers in pharmacology · 2025Article
- Expression of Multiple Copies of the Lon Protease Gene Resulted in Increased Antibiotic Production, Osmotic and UV Stress Resistance in Streptomyces coelicolor A3(2).Current microbiology · 2024Article
- Allosteric modulation of the Lon protease by effector binding and local charges.bioRxiv : the preprint server for biology · 2024Article
- Allelic variations in the chpG effector gene within Clavibacter michiganensis populations determine pathogen host range.PLoS pathogens · 2024Article
- Regulation of the general stress response sigma factor σJournal of bacteriology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The Lon protease is a highly conserved protein degradation machine that has critical regulatory and protein quality control functions in cells from the three domains of life. Here, we report the discovery of a α-proteobacterial heat shock protein, LarA, that functions as a dedicated Lon regulator. We show that LarA accumulates at the onset of proteotoxic stress and allosterically activates Lon-catalysed degradation of a large group of substrates through a five amino acid sequence at its C-terminus. Further, we find that high levels of LarA cause growth inhibition in a Lon-dependent manner and that Lon-mediated degradation of LarA itself ensures low LarA levels in the absence of stress. We suggest that the temporal LarA-dependent activation of Lon helps to meet an increased proteolysis demand in response to protein unfolding stress. Our study defines a regulatory interaction of a conserved protease with a heat shock protein, serving as a paradigm of how protease activity can be tuned under changing environmental conditions.
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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.