ArticleMolecular cell2017
HspQ Functions as a Unique Specificity-Enhancing Factor for the AAA+ Lon Protease.
Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed.
- An adaptor for feedback regulation of heme biosynthesis by a mitochondrial protease.Science (New York, N.Y.) · 2026Article
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Mrx6 binds the Lon protease Pim1 N-terminal domain to confer selective substrate specificity and regulate mtDNA copy number.Nucleic acids research · 2026Article
- A Proteomic View on Persistence of Yersinia pestis in Tap Water Microcosm.Current microbiology · 2025Article
- Autophagy and the Mitochondrial Lon1 Protease Are Necessary for Botrytis cinerea Heat Adaptation.Molecular microbiology · 2025Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- Structural basis for the allosteric activation of Lon by the heat shock protein LarA.Nature communications · 2025Article
- Allosteric modulation of the Lon protease by effector binding and local charges.bioRxiv : the preprint server for biology · 2024Article
- The heat shock protein LarA activates the Lon protease in response to proteotoxic stress.Nature communications · 2023Article
- A sporulation signature protease is required for assembly of the spore surface layers, germination and host colonization in Clostridioides difficile.PLoS pathogens · 2023Article
- Advancing evolution: Bacteria break down gene silencer to express horizontally acquired genes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Article
- Mitochondrial Dysfunction Associated with mtDNA in Metabolic Syndrome and Obesity.International journal of molecular sciences · 2023Review
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Evidence for mitochondrial Lonp1 expression in the nucleus.Scientific reports · 2022Article
- Degron-mediated proteolysis of CrhR-like DEAD-box RNA helicases in cyanobacteria.The Journal of biological chemistry · 2022Article
- Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.FEBS letters · 2021Article
- Article
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
- Nucleoid-associated proteins shape chromatin structure and transcriptional regulation across the bacterial kingdom.Transcription · 2021Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The AAA+ Lon protease is conserved from bacteria to humans, performs crucial roles in protein homeostasis, and is implicated in bacterial pathogenesis and human disease. We investigated how Lon selectively degrades specific substrates among a diverse array of potential targets. We report the discovery of HspQ as a new Lon substrate, unique specificity-enhancing factor, and potent allosteric activator. Lon recognizes HspQ via a C-terminal degron, whose precise presentation, in synergy with multipartite contacts with the native core of HspQ, is required for allosteric Lon activation. Productive HspQ-Lon engagement enhances degradation of multiple new and known Lon substrates. Our studies reveal the existence and simultaneous utilization of two distinct substrate recognition sites on Lon, an HspQ binding site and an HspQ-modulated allosteric site. Our investigations unveil an unprecedented regulatory use of an evolutionarily conserved heat shock protein and present a distinctive mechanism for how Lon protease achieves temporally enhanced substrate selectivity.
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Registered trials
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.