ArticleNature communications2024
Structure of cryptophyte photosystem II-light-harvesting antennae supercomplex.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- pH-Dependent Vibrational Dynamics Drives Excited-State Quenching in the Phycobiliprotein Complex PC645.Journal of the American Chemical Society · 2026Article
- Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance.Nature communications · 2026Article
- Widely targeted metabolomic and transcriptomic analyses of the effects of blue polarized light and ordinary light onFrontiers in plant science · 2026Article
- Architecture and energy transfer of coccolithophore photosystem I with a huge light-harvesting antenna system.Science advances · 2025Article
- Photosystem II: commonality and diversity with emphasis on the extrinsic subunits.Plant & cell physiology · 2025Review
- Histone ZmH2B regulates resistance to the Southern corn leaf blight pathogen Bipolaris maydis in maize.BMC plant biology · 2025Article
- The lumenal domain of Cyt bPhotosynthesis research · 2025Article
- Structure of a photosystem II-FCPII supercomplex from a haptophyte reveals a distinct antenna organization.Nature communications · 2025Article
- Structural analysis of PSI-ACPI and PSII-ACPII supercomplexes from a cryptophyte algaFrontiers in plant science · 2025Article
- Structural insights into the assembly and energy transfer of haptophyte photosystem I-light-harvesting supercomplex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis for the distinct core-antenna assembly of cryptophyte photosystem II.Nature communications · 2024Article
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Authors and funding
10 authors.
Funding
Abstract
Cryptophytes are ancestral photosynthetic organisms evolved from red algae through secondary endosymbiosis. They have developed alloxanthin-chlorophyll a/c2-binding proteins (ACPs) as light-harvesting complexes (LHCs). The distinctive properties of cryptophytes contribute to efficient oxygenic photosynthesis and underscore the evolutionary relationships of red-lineage plastids. Here we present the cryo-electron microscopy structure of the Photosystem II (PSII)-ACPII supercomplex from the cryptophyte Chroomonas placoidea. The structure includes a PSII dimer and twelve ACPII monomers forming four linear trimers. These trimers structurally resemble red algae LHCs and cryptophyte ACPI trimers that associate with Photosystem I (PSI), suggesting their close evolutionary links. We also determine a Chl a-binding subunit, Psb-γ, essential for stabilizing PSII-ACPII association. Furthermore, computational calculation provides insights into the excitation energy transfer pathways. Our study lays a solid structural foundation for understanding the light-energy capture and transfer in cryptophyte PSII-ACPII, evolutionary variations in PSII-LHCII, and the origin of red-lineage LHCIIs.
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