ArticleFrontiers in plant science2014
Localization of the CyanoP binding site on photosystem II by surface plasmon resonance spectroscopy.
Article in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 28 citations in OpenAlex.
- Exploring thylakoid emergence: evolution of membrane biogenesis and photosystem II assembly in early-diverging cyanobacteria.The New phytologist · 2026Article
- Exploring Thylakoid Emergence: Evolution of Membrane Biogenesis and Photosystem II assembly in early-diverging Cyanobacteria.bioRxiv : the preprint server for biology · 2026Article
- Photosystem II: commonality and diversity with emphasis on the extrinsic subunits.Plant & cell physiology · 2025Review
- The lumenal domain of Cyt bPhotosynthesis research · 2025Article
- Binding and functions of the two chloride ions in the oxygen-evolving center of photosystem II.Photosynthesis research · 2022Review
- Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins.Plant physiology · 2022Article
- Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium.Nature communications · 2022Article
- The Photosystem II Assembly Factor Ycf48 from the CyanobacteriumInternational journal of molecular sciences · 2021Article
- The extrinsic proteins of photosystem II: update.Planta · 2016Review
- The N-terminal sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II.Scientific reports · 2016Article
- Environmental pH and the Requirement for the Extrinsic Proteins of Photosystem II in the Function of Cyanobacterial Photosynthesis.Frontiers in plant science · 2016Article
- Structural Coupling of Extrinsic Proteins with the Oxygen-Evolving Center in Photosystem II.Frontiers in plant science · 2016Review
- The Role of Slr0151, a Tetratricopeptide Repeat Protein from Synechocystis sp. PCC 6803, during Photosystem II Assembly and Repair.Frontiers in plant science · 2016Article
- Critical Assessment of Protein Cross-Linking and Molecular Docking: An Updated Model for the Interaction Between Photosystem II and Psb27.Frontiers in plant science · 2016Article
- Characterization of a Synechocystis sp. PCC 6803 double mutant lacking the CyanoP and Ycf48 proteins of Photosystem II.Photosynthesis research · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosystem II (PSII), a large multi subunit membrane protein complex localized in the thylakoid membrane of cyanobacteria and chloroplasts, is the only known enzyme that catalyzes the light-driven oxidation of water. In addition to the membrane intrinsic part of PSII, efficient oxygen evolution requires soluble protein subunits at its luminal interface. In contrast to the detailed crystal structure of the active cyanobacterial complex the characterization of intermediate PSII species related to its assembly and repair is hampered by their instability or low abundance. As most structural variations of the corresponding PSII species are based on a different set of protein factors bound to the luminal interface of the complex we developed a system for interaction analysis between PSII and its soluble interaction partners based on surface plasmon resonance (SPR) spectroscopy. The assay was validated by the correct localization of the extrinsic PSII proteins PsbO, PsbV, and PsbU on the luminal PSII surface and used to determine the unknown binding position of CyanoP, the cyanobacterial homolog of higher plant PsbP. The CyanoP binding site was clearly localized in the center of PSII at a position, which is occupied by the PsbO subunit in mature PSII complexes. Consistently, we demonstrate selective binding of CyanoP to an inactive PSII assembly intermediate that lacks the extrinsic subunits PsbO, PsbV, and PsbU. These findings suggest, that CyanoP functions in the dynamic lifecycle of PSII, possibly in the association of CP47 and CP43 or in photoactivation of the oxygen-evolving complex.
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