ArticleBMC evolutionary biology2010
Chlorophyll-binding proteins revisited--a multigenic family of light-harvesting and stress proteins from a brown algal perspective.
Article in BMC evolutionary biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 124 citations in OpenAlex.
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- Chlorophyll a/b-binding protein gene AcLhcb1.1 promotes chlorophyll accumulation and improves cold stress resistance in kiwifruit.BMC plant biology · 2025Article
- Pennate diatoms make non-photochemical quenching as simple as possible but not simpler.Nature communications · 2025Article
- Unraveling the evolutionary trajectory of LHCI in red-lineage algae: Conservation, diversification, and neolocalization.iScience · 2024Article
- Multifaceted natural drought response mechanisms in three elite date palm cultivars uncovered by expressed sequence tags analysis.Scientific reports · 2024Article
- Organellar Genomes ofInternational journal of molecular sciences · 2024Article
- Salinity Stress Acclimation Strategies inMarine drugs · 2024Article
- Physiochemical and molecular responses of the diatom Phaeodactylum tricornutum to illumination transitions.Biotechnology for biofuels and bioproducts · 2023Article
- A spatiotemporal atlas of organogenesis in the development of orchid flowers.Nucleic acids research · 2022Article
- Multi-Omics Profiling Reveals Resource Allocation and Acclimation Strategies to Temperature Changes in a Marine Dinoflagellate.Applied and environmental microbiology · 2022Article
- Biochemical and molecular properties of LHCX1, the essential regulator of dynamic photoprotection in diatoms.Plant physiology · 2022Article
- Transcriptomic and Metabolomic Response to High Light in the Charophyte AlgaFrontiers in plant science · 2022Article
- OsCpn60β1 is Essential for Chloroplast Development in Rice (International journal of molecular sciences · 2020Article
- Article
- Red-shifted light-harvesting system of freshwater eukaryotic alga Trachydiscus minutus (Eustigmatophyta, Stramenopila).Photosynthesis research · 2019Article
- Light-harvesting protein Lhcx3 is essential for high light acclimation of Phaeodactylum tricornutum.AMB Express · 2018Article
- Quenching of chlorophyll triplet states by carotenoids in algal light-harvesting complexes related to fucoxanthin-chlorophyll protein.Photosynthesis research · 2018Article
- Red-light phenotype in a marine diatom involves a specialized oligomeric red-shifted antenna and altered cell morphology.Scientific reports · 2017Article
- Chimeric origins of ochrophytes and haptophytes revealed through an ancient plastid proteome.eLife · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundChlorophyll-binding proteins (CBPs) constitute a large family of proteins with diverse functions in both light-harvesting and photoprotection. The evolution of CBPs has been debated, especially with respect to the origin of the LI818 subfamily, members of which function in non-photochemical quenching and have been found in chlorophyll a/c-containing algae and several organisms of the green lineage, but not in red algae so far. The recent publication of the Ectocarpus siliculosus genome represents an opportunity to expand on previous work carried out on the origin and function of CBPs.
resultsThe Ectocarpus genome codes for 53 CBPs falling into all major families except the exclusively green family of chlorophyll a/b binding proteins. Most stress-induced CBPs belong to the LI818 family. However, we highlight a few stress-induced CBPs from Phaeodactylum tricornutum and Chondrus crispus that belong to different sub-families and are promising targets for future functional studies. Three-dimensional modeling of two LI818 proteins revealed features common to all LI818 proteins that are likely to interfere with their capacity to bind chlorophyll b and lutein, but may enable binding of chlorophyll c and fucoxanthin. In the light of this finding, we examined the possibility that LI818 proteins may have originated in a chlorophyll c/fucoxanthin containing organism and compared this scenario to three alternatives: an independent evolution of LI818 proteins in different lineages, an ancient origin together with the first CBPs, before the separation of the red and the green lineage, or an origin in the green lineage and a transfer to an ancestor of haptophytes and heterokonts during a cryptic endosymbiosis event.
conclusionsOur findings reinforce the idea that the LI818 family of CBPs has a role in stress response. In addition, statistical analyses of phylogenetic trees show an independent origin in different eukaryotic lineages or a green algal origin of LI818 proteins to be highly unlikely. Instead, our data favor an origin in an ancestral chlorophyll a/c-containing organism and a subsequent lateral transfer to some green algae, although an origin of LI818 proteins in a common ancestor of red and green algae cannot be ruled out.
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