ArticlePloS one2012
Biological roles of the Podospora anserina mitochondrial Lon protease and the importance of its N-domain.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Autophagy and the Mitochondrial Lon1 Protease Are Necessary for Botrytis cinerea Heat Adaptation.Molecular microbiology · 2025Article
- What are the 100 most cited fungal genera?Studies in mycology · 2024Article
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Article
- A Network of Pathways Controlling Cellular Homeostasis Affects the Onset of Senescence inJournal of fungi (Basel, Switzerland) · 2021Review
- The Glyoxysomal Protease LON2 Is Involved in Fruiting-Body Development, Ascosporogenesis and Stress Resistance inJournal of fungi (Basel, Switzerland) · 2021Article
- Simultaneous Ablation of the Catalytic AMPK α-Subunit SNF1 and Mitochondrial Matrix Protease CLPP Results in Pronounced Lifespan Extension.Frontiers in cell and developmental biology · 2021Article
- The C3HC type zinc-finger protein (ZFC3) interacting with Lon/MAP1 is important for mitochondrial gene regulation, infection hypha development and longevity of Magnaporthe oryzae.BMC microbiology · 2020Article
- Quercetin-Induced Lifespan Extension inFrontiers in genetics · 2018Article
- The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.Scientific reports · 2016Article
- Characterization of the aodA, dnmA, mnSOD and pimA genes in Aspergillus nidulans.Scientific reports · 2016Article
- Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer.Cellular and molecular life sciences : CMLS · 2015Review
- Proteins interacting with mitochondrial ATP-dependent Lon protease (MAP1) in Magnaporthe oryzae are involved in rice blast disease.Molecular plant pathology · 2015Article
- Control of mitochondrial integrity in ageing and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Identification of autophagy as a longevity-assurance mechanism in the aging model Podospora anserina.Autophagy · 2014Article
- Linkage of oxidative stress and mitochondrial dysfunctions to spontaneous culture degeneration in Aspergillus nidulans.Molecular & cellular proteomics : MCP · 2014Article
- Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.Molecular microbiology · 2014Article
- Mitochondrial aging and age-related dysfunction of mitochondria.BioMed research international · 2014Review
- Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain.Nature communications · 2013Article
- Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondria have their own ATP-dependent proteases that maintain the functional state of the organelle. All multicellular eukaryotes, including filamentous fungi, possess the same set of mitochondrial proteases, unlike in unicellular yeasts, where ClpXP, one of the two matricial proteases, is absent. Despite the presence of ClpXP in the filamentous fungus Podospora anserina, deletion of the gene encoding the other matricial protease, PaLon1, leads to lethality at high and low temperatures, indicating that PaLON1 plays a main role in protein quality control. Under normal physiological conditions, the PaLon1 deletion is viable but decreases life span. PaLon1 deletion also leads to defects in two steps during development, ascospore germination and sexual reproduction, which suggests that PaLON1 ensures important regulatory functions during fungal development. Mitochondrial Lon proteases are composed of a central ATPase domain flanked by a large non-catalytic N-domain and a C-terminal protease domain. We found that three mutations in the N-domain of PaLON1 affected fungal life cycle, PaLON1 protein expression and mitochondrial proteolytic activity, which reveals the functional importance of the N-domain of the mitochondrial Lon protease. All PaLon1 mutations affected the C-terminal part of the N-domain. Considering that the C-terminal part is predicted to have an α helical arrangement in which the number, length and position of the helices are conserved with the solved structure of its bacterial homologs, we propose that this all-helical structure participates in Lon substrate interaction.
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