ArticleThe Plant cell2000
The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein.
Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.
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139 citing papers in PubMed, 391 citations in OpenAlex.
- Leaf variegation in a barley EMS mutant is controlled by two epistatic mutations.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Article
- Trp521 oxidation affects FtsH2 stability and its role in PSII repair.The New phytologist · 2026Article
- Article
- Chloroplastic protein PORC undergoes heat-induced condensation and enhances thermotolerance in Arabidopsis.Plant physiology · 2026Article
- The GreenCut protein TEF6 maintains photosystem II homeostasis under high light by stabilizing FtsH accumulation in Chlamydomonas reinhardtii.Plant communications · 2026Article
- Comparative genome-wide analysis in Setaria italica and Arabidopsis thaliana revealed functional conservation of specific FtsH proteases under high light and heat stress.Plant cell reports · 2026Article
- Heat Shock Transcription Factor OsHsfc1a Enhances Rice Seedling Thermotolerance by Regulating OsMFT1 and Preserving Chloroplast Structure Under Heat Stress.Plant biotechnology journal · 2026Article
- What are grana in chloroplasts of vascular plants good for?Annals of botany · 2026Review
- Identification of theFrontiers in plant science · 2026Article
- Overexpression of theFrontiers in genetics · 2026Article
- Chloroplast Responses to Drought: Integrative Mechanisms and Mitigation Strategies.International journal of molecular sciences · 2025Review
- Roles of multiple TEF30-associated intermediate complexes in the repair and reassembly of photosystem II in Chlamydomonas reinhardtii.Nature plants · 2025Article
- Chloroplast ATP-dependent metalloprotease FtsH5/VAR1 confers cold-stress tolerance through singlet oxygen and salicylic acid signaling.Plant communications · 2025Article
- The thylakoid lumen Deg1 protease affects non-photochemical quenching via the levels of violaxanthin de-epoxidase and PsbS.The Plant journal : for cell and molecular biology · 2025Article
- Fixing PSII: Membrane fluidity facilitates FtsH functions.The Plant cell · 2024Article
- Temperature-driven changes in membrane fluidity differentially impact FILAMENTATION TEMPERATURE-SENSITIVE H2-mediated photosystem II repair.The Plant cell · 2024Article
- Reduced plastid genomes of colorless facultative pathogens Prototheca (Chlorophyta) are retained for membrane transport genes.BMC biology · 2024Article
- Lighting the way: Compelling open questions in photosynthesis research.The Plant cell · 2024Article
- Article
- Chloroplast SRP54 and FtsH protease coordinate thylakoid membrane-associated proteostasis in Arabidopsis.Plant physiology · 2023Article
79 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The photosystem II reaction center D1 protein is known to turn over frequently. This protein is prone to irreversible damage caused by reactive oxygen species that are formed in the light; the damaged, nonfunctional D1 protein is degraded and replaced by a new copy. However, the proteases responsible for D1 protein degradation remain unknown. In this study, we investigate the possible role of the FtsH protease, an ATP-dependent zinc metalloprotease, during this process. The primary light-induced cleavage product of the D1 protein, a 23-kD fragment, was found to be degraded in isolated thylakoids in the dark during a process dependent on ATP hydrolysis and divalent metal ions, suggesting the involvement of FtsH. Purified FtsH degraded the 23-kD D1 fragment present in isolated photosystem II core complexes, as well as that in thylakoid membranes depleted of endogenous FtsH. In this study, we definitively identify the chloroplast protease acting on the D1 protein during its light-induced turnover. Unlike previously identified membrane-bound substrates for FtsH in bacteria and mitochondria, the 23-kD D1 fragment represents a novel class of FtsH substrate-functionally assembled proteins that have undergone irreversible photooxidative damage and cleavage.
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