ArticleProceedings of the National Academy of Sciences of the United States of America2016
Orange carotenoid protein burrows into the phycobilisome to provide photoprotection.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 93 citations in OpenAlex.
- Atomistic simulations reveal the photoactivation mechanism of a carotenoid-binding photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Orange Carotenoid Protein Triggers Cyanobacterial Photoprotection by Quenching Bilins via a Structural Switch of Its Carotenoid.Journal of the American Chemical Society · 2024Article
- Structure and function of the light-protective orange carotenoid protein families.Current research in structural biology · 2024Review
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Article
- A kaleidoscope of photosynthetic antenna proteins and their emerging roles.Plant physiology · 2022Article
- A favorable path to domain separation in the orange carotenoid protein.Protein science : a publication of the Protein Society · 2022Article
- Light quality, oxygenic photosynthesis and more.Photosynthetica · 2022Review
- Structural insight into the mechanism of energy transfer in cyanobacterial phycobilisomes.Nature communications · 2021Article
- Inverse regulation of light harvesting and photoprotection is mediated by a 3'-end-derived sRNA in cyanobacteria.The Plant cell · 2021Article
- Mechanical regulation of photosynthesis in cyanobacteria.Nature microbiology · 2020Article
- X-ray radiolytic labeling reveals the molecular basis of orange carotenoid protein photoprotection and its interactions with fluorescence recovery protein.The Journal of biological chemistry · 2019Article
- Single-molecule trapping and spectroscopy reveals photophysical heterogeneity of phycobilisomes quenched by Orange Carotenoid Protein.Nature communications · 2019Article
- Photoactivation Mechanism, Timing of Protein Secondary Structure Dynamics and Carotenoid Translocation in the Orange Carotenoid Protein.Journal of the American Chemical Society · 2019Article
- Roles of CpcF and CpcG1 in Peroxiredoxin-Mediated Oxidative Stress Responses and Cellular Fitness in the CyanobacteriumFrontiers in microbiology · 2019Article
- OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.Nature communications · 2018Article
- Site, trigger, quenching mechanism and recovery of non-photochemical quenching in cyanobacteria: recent updates.Photosynthesis research · 2018Review
- Structural integrity of Synechocystis sp. PCC 6803 phycobilisomes evaluated by means of differential scanning calorimetry.Photosynthesis research · 2018Article
- Photoprotective, excited-state quenching mechanisms in diverse photosynthetic organisms.The Journal of biological chemistry · 2018Review
- Photoactivation and relaxation studies on the cyanobacterial orange carotenoid protein in the presence of copper ion.Photosynthesis research · 2018Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In cyanobacteria, photoprotection from overexcitation of photochemical centers can be obtained by excitation energy dissipation at the level of the phycobilisome (PBS), the cyanobacterial antenna, induced by the orange carotenoid protein (OCP). A single photoactivated OCP bound to the core of the PBS affords almost total energy dissipation. The precise mechanism of OCP energy dissipation is yet to be fully determined, and one question is how the carotenoid can approach any core phycocyanobilin chromophore at a distance that can promote efficient energy quenching. We have performed intersubunit cross-linking using glutaraldehyde of the OCP and PBS followed by liquid chromatography coupled to tandem mass spectrometry (LC/MS-MS) to identify cross-linked residues. The only residues of the OCP that cross-link with the PBS are situated in the linker region, between the N- and C-terminal domains and a single C-terminal residue. These links have enabled us to construct a model of the site of OCP binding that differs from previous models. We suggest that the N-terminal domain of the OCP burrows tightly into the PBS while leaving the OCP C-terminal domain on the exterior of the complex. Further analysis shows that the position of the small core linker protein ApcC is shifted within the cylinder cavity, serving to stabilize the interaction between the OCP and the PBS. This is confirmed by a ΔApcC mutant. Penetration of the N-terminal domain can bring the OCP carotenoid to within 5-10 Å of core chromophores; however, alteration of the core structure may be the actual source of energy dissipation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.