ArticleFrontiers in plant science2021
Conserved Residues in the C-Terminal Domain Affect the Structure and Function of CYP38 in Arabidopsis.
Article in Frontiers in plant science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Comprehensive identification of glutathione peroxidase (GPX) gene family and effect of GhGPX4 on reactive oxygen species metabolism in cotton.Frontiers in plant science · 2026Article
- Characterization of Arabidopsis thaliana thylakoid lumen 7.6 protein functions in photosystem II assembly.Communications biology · 2025Article
- Adaptive responses of plants to light stress: mechanisms of photoprotection and acclimation. A review.Frontiers in plant science · 2025Review
- Immunophilin CYN28 is required for accumulation of photosystem II and thylakoid FtsH protease in Chlamydomonas.Plant physiology · 2023Article
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
Arabidopsis cyclophilin38 (CYP38) is a thylakoid lumen protein critial for PSII assembly and maintenance, and its C-terminal region serves as the target binding domain. We hypothesized that four conserved residues (R290, F294, Q372, and F374) in the C-terminal domain are critical for the structure and function of CYP38. In yeast two-hybrid and protein pull-down assays, CYP38s with single-sited mutations (R290A, F294A, Q372A, or F374A) did not interact with the CP47 E-loop as the wild-type CYP38. In contrast, CYP38 with the R290A/F294A/Q372A/F374A quadruple mutation could bind the CP47 E-loop. Gene transformation analysis showed that the quadruple mutation prevented CYP38 to efficiently complement the mutant phenotype of
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