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The D1 and D2 proteins of dinoflagellates: unusually accumulated mutations which influence on PSII photoreaction

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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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Abbreviations

a. a.:

Amino acid

cDNA:

DNA complementary to RNA

Chl:

Chlorophyll

C-terminus:

Carboxyl terminus

DCMU:

3-(3,4-Dichlorophenyl)-1,1-dimethylurea

F V :

Variable fluorescence

F M :

Maximum fluorescence

N-terminus:

Amino terminus

PSII:

Photosystem II

Rubisco:

Ribulose 1,5-bisphosphate carboxylase/oxygenase

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Acknowledgments

We thank Drs. M. Mimuro and T. Tomo (Kyoto University) for the permission to use Dual-Modulation Kinetic Fluorometer and Ms. H. Uchida (Kobe University) for preparation of figure illustrations. We also appreciate Research Center for Environmental Genomics (Kobe University) for assistance in DNA sequencing. Present work was supported by a Grant-in-Aid for Creative Scientific Research from the Japan Society for the Promotion of Science to A.M. (No. 17GS0314) and a Kurita Water and Environment Foundation Grant to S.I.

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Authors and Affiliations

  1. Kobe University Research Center for Inland Seas, Iwaya 2746, Awaji, Hyogo, 656-2401, Japan

    Satoko Iida & Akio Murakami

  2. School of Marine Biosciences, Kitasato University, Sanriku, Ofunato, Iwate, 022-0101, Japan

    Atsushi Kobiyama & Takehiko Ogata

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  1. Satoko Iida
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  2. Atsushi Kobiyama
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  3. Takehiko Ogata
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  4. Akio Murakami
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Correspondence to Akio Murakami.

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Iida, S., Kobiyama, A., Ogata, T. et al. The D1 and D2 proteins of dinoflagellates: unusually accumulated mutations which influence on PSII photoreaction. Photosynth Res 98, 415–425 (2008). https://doi.org/10.1007/s11120-008-9378-y

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