ArticlePhotosynthesis research
The D1 and D2 proteins of dinoflagellates: unusually accumulated mutations which influence on PSII photoreaction.
Article in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Integrative Physiological, Transcriptome, and Proteome Analyses Provide Insights into the Photosynthetic Changes in Maize in a Maize-Peanut Intercropping System.Plants (Basel, Switzerland) · 2023Article
- The photosynthetic function analysis for leaf photooxidation in rice.Photosynthetica · 2023Article
- Enhancement of exopolysaccharides production and reactive oxygen species level of Nostoc flagelliforme in response to dehydration.Environmental science and pollution research international · 2021Article
- Adaptive divergence, neutral panmixia, and algal symbiont population structure in the temperate coralPeerJ · 2020Article
- Transcriptomic Analysis of Thermally StressedFrontiers in plant science · 2017Article
- Excitation relaxation dynamics and energy transfer in pigment-protein complexes of a dinoflagellate, revealed by ultrafast fluorescence spectroscopy.Photosynthesis research · 2016Article
- The PsbO homolog from Symbiodinium kawagutii (Dinophyceae) characterized using biochemical and molecular methods.Photosynthesis research · 2013Article
- Identification of transcribed and persistent variants of the psbA gene carried by plastid minicircles in a dinoflagellate.Current genetics · 2009Article
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Authors and funding
4 authors.
Funding
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Abstract
Plastid encoded genes of the dinoflagellates are rapidly evolving and most divergent. The importance of unusually accumulated mutations on structure of PSII core protein and photosynthetic function was examined in the dinoflagellates, Symbiodinium sp. and Alexandrium tamarense. Full-length cDNA sequences of psbA (D1 protein) and psbD (D2 protein) were obtained and compared with the other oxygen-evolving photoautotrophs. Twenty-three amino acid positions (7%) for the D1 protein and 34 positions (10%) for the D2 were mutated in the dinoflagellates, although amino acid residues at these positions were conserved in cyanobacteria, the other algae, and plant. Many mutations were likely to distribute in the N-terminus and the D-E interhelical loop of the D1 protein and helix B of D2 protein, while the remaining regions were well conserved. The different structural properties in these mutated regions were supported by hydropathy profiles. The chlorophyll fluorescence kinetics of the dinoflagellates was compared with Synechocystis sp. PCC6803 in relation to the altered protein structure.
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