ArticlePhotosynthesis research2012
Phylogenetic analysis of the light-harvesting system in Chromera velia.
Article in Photosynthesis research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 34 citations in OpenAlex.
- The cryo-EM structure of Photosystem I from Chromera velia with a bound superoxide dismutase heterodimer.Nature communications · 2025Article
- Far-red light acclimation in diverse oxygenic photosynthetic organisms.Photosynthesis research · 2019Review
- Antenna proton sensitivity determines photosynthetic light harvesting strategy.Journal of experimental botany · 2018Article
- Extensive gain and loss of photosystem I subunits in chromerid algae, photosynthetic relatives of apicomplexans.Scientific reports · 2017Article
- Modular antenna of photosystem I in secondary plastids of red algal origin: a Nannochloropsis oceanica case study.Photosynthesis research · 2017Article
- A two-component nonphotochemical fluorescence quenching in eustigmatophyte algae.Photosynthesis research · 2017Article
- Unusual features of the high light acclimation of Chromera velia.Photosynthesis research · 2014Article
- Evidence of intraflagellar transport and apical complex formation in a free-living relative of the apicomplexa.Eukaryotic cell · 2014Article
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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
Chromera velia is a newly discovered photosynthetic eukaryotic alga that has functional chloroplasts closely related to the apicoplast of apicomplexan parasites. Recently, the chloroplast in C. velia was shown to be derived from the red algal lineage. Light-harvesting protein complexes (LHC), which are a group of proteins involved in photon capture and energy transfer in photosynthesis, are important for photosynthesis efficiency, photo-adaptation/accumulation and photo-protection. Although these proteins are encoded by genes located in the nucleus, LHC peptides migrate and function in the chloroplast, hence the LHC may have a different evolutionary history compared to chloroplast evolution. Here, we compare the phylogenetic relationship of the C. velia LHCs to LHCs from other photosynthetic organisms. Twenty-three LHC homologues retrieved from C. velia EST sequences were aligned according to their conserved regions. The C. velia LHCs are positioned in four separate groups on trees constructed by neighbour-joining, maximum likelihood and Bayesian methods. A major group of seventeen LHCs from C. velia formed a separate cluster that was closest to dinoflagellate LHC, and to LHC and fucoxanthin chlorophyll-binding proteins from diatoms. One C. velia LHC sequence grouped with LI1818/LI818-like proteins, which were recently identified as environmental stress-induced protein complexes. Only three LHC homologues from C. velia grouped with the LHCs from red algae.
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