ArticlePlant physiology2021
The mitochondrial AAA protease FTSH3 regulates Complex I abundance by promoting its disassembly.
Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Genome-wide identification and characterization of filamentation temperature-sensitive H (FtsH) genes and expression analysis in response to multiple stresses in Medicago truncatula.Molecular biology reports · 2023Article
- FTSH PROTEASE 3 facilitates Complex I degradation through a direct interaction with the Complex I subunit PSST.The Plant cell · 2023Article
- Mitochondrial respiratory complex I proteostasis: The role of a subunit turnover rate.The Plant cell · 2023Article
- The biogenesis and regulation of the plant oxidative phosphorylation system.Plant physiology · 2023Review
- Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants.Biochemical Society transactions · 2022Review
- The mitochondrial LYR protein SDHAF1 is required for succinate dehydrogenase activity in Arabidopsis.The Plant journal : for cell and molecular biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP is generated in mitochondria by oxidative phosphorylation. Complex I (NADH:ubiquinone oxidoreductase or NADH dehydrogenase) is the first multisubunit protein complex of this pathway, oxidizing NADH and transferring electrons to the ubiquinone pool. Typically, Complex I mutants display a slow growth rate compared to wild-type plants. Here, using a forward genetic screen approach for restored growth of a Complex I mutant, we have identified the mitochondrial ATP-dependent metalloprotease, Filamentous Temperature Sensitive H 3 (FTSH3), as a factor that is required for the disassembly of Complex I. An ethyl methanesulfonate-induced mutation in FTSH3, named as rmb1 (restoration of mitochondrial biogenesis 1), restored Complex I abundance and plant growth. Complementation could be achieved with FTSH3 lacking proteolytic activity, suggesting the unfoldase function of FTSH3 has a role in Complex I disassembly. The introduction of the rmb1 to an additional, independent, and extensively characterized Complex I mutant, ndufs4, resulted in similar increases to Complex I abundance and a partial restoration of growth. These results show that disassembly or degradation of Complex I plays a role in determining its steady-state abundance and thus turnover may vary under different conditions.
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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.