ArticlePlant physiology2023
Immunophilin CYN28 is required for accumulation of photosystem II and thylakoid FtsH protease in Chlamydomonas.
Article in Plant physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- OsFT coordinates photosynthetic stability and carotenoid metabolism to regulate tillering in rice.Journal of advanced research · 2026Article
- Light-induced increase in the steady-state chlorophyll fluorescence in cyanobacteria reflects induction of energy dissipation complementary to orange carotenoid protein-dependent thermal dissipation.Photosynthesis research · 2025Article
- A game of tag: A review of protein tags for the successful detection, purification and fluorescence labelling of proteins expressed in microalgae.The Plant journal : for cell and molecular biology · 2025Review
- The biogenesis and maintenance of PSII: Recent advances and current challenges.The Plant cell · 2024Review
- The Role of FtsH Complexes in the Response to Abiotic Stress in Cyanobacteria.Plant & cell physiology · 2024Review
- Advances in light system engineering across the phototrophic spectrum.Frontiers in plant science · 2024Review
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Excess light causes severe photodamage to photosystem II (PSII) where the primary charge separation for electron transfer takes place. Dissection of mechanisms underlying the PSII maintenance and repair cycle in green algae promotes the usage of genetic engineering and synthetic biology to improve photosynthesis and biomass production. In this study, we systematically analyzed the high light (HL) responsive immunophilin genes in Chlamydomonas (Chlamydomonas reinhardtii) and identified one chloroplast lumen-localized immunophilin, CYN28, as an essential player in HL tolerance. Lack of CYN28 caused HL hypersensitivity, severely reduced accumulation of PSII supercomplexes and compromised PSII repair in cyn28. The thylakoid FtsH (filamentation temperature-sensitive H) is an essential AAA family metalloprotease involved in the degradation of photodamaged D1 during the PSII repair cycle and was identified as one potential target of CYN28. In the cyn28 mutant, the thylakoid FtsH undergoes inefficient turnover under HL conditions. The CYN28-FtsH1/2 interaction relies on the FtsH N-terminal proline residues and is strengthened particularly under HL. Further analyses demonstrated CYN28 displays peptidyl-prolyl isomerase (PPIase) activity, which is necessary for its physiological function. Taken together, we propose that immunophilin CYN28 participates in PSII maintenance and regulates the homeostasis of FtsH under HL stress via its PPIase activity.
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