Identification of genes encoding photoconvertible (Class I) water-soluble chlorophyll-binding proteins from Chenopodium ficifolium

References

• Satoh H, Uchida A, Nakayama K, Okada M. Water-soluble chlorophyll protein in Brassicaceae plants is a stress-induced chlorophyll-binding protein. Plant Cell Physiol. 2001;42:906–911.10.1093/pcp/pce117
   PubMed Web of Science ®Google Scholar
• Takamiya A. Distribution of photoconvertible water-soluble chlorophyll protein complex CP668 in plants related to Chenopodium album. Carnegie Inst. Yearbook. 1973;72:330–336.
   Google Scholar
• Goedheer JC, Vos M. On the origin of the photoconvertible chlorophyll–protein complex Cp668 → Cp743 in Chenopodium and Amaranthus species. Acta Bot. Neerl. 1977;26:289–298.
   Google Scholar
• Takahashi S, Satoh H. Mini-review of the molecular properties and physiological functions of non-photoconvertible water-soluble chlorophyll-binding proteins (WSCPs) in Brassicaceae plants. In: Lang M, editor. Brassicaceae: characterization, functional genomics and health benefits. New York (NY): Nova Science Publishers; 2013. p. 111–120.
   Google Scholar
• Yakushiji E, Uchino K, Sugimura Y, Shiratori I, Takamiya F. Isolation of water-soluble chlorophyll protein from the leaves of Chenopodium album. Biochim. Biophys. Acta. 1963;75:293–298.10.1016/0006-3002(63)90615-2
   PubMed Web of Science ®Google Scholar
• Terpstra W. Experiments on the extraction and photoconversion of Chenopodium chlorophyll protein CP 668. Biochim. Biophys. Acta. 1966;120:317–325.10.1016/0926-6585(66)90298-6
   PubMed Web of Science ®Google Scholar
• Murata T, Odaka Y, Uchino K, Yakushiji E. Reconstitution of the photo-sensitive form of Chenopodium chlorophyll protein from its apoprotein. In: Shibata K, Takamiya A, Jagendorf AT, Fuller RC, editors. Comparative biochemistry and biophysics of photosynthesis. Tokyo: University of Tokyo Press; 1968. p. 222–228.
   Google Scholar
• Takamiya A, Kamimura Y, Kira A. A transient form of chlorophyll produced by flash photolysis of Chenopodium chlorophyll protein, CP668. In: Shibata K, Takamiya A, Jagendorf AT, Fuller RC, editors. Comparative biochemistry and biophysics of photosynthesis. Tokyo: University of Tokyo Press; 1968. p. 229–239.
   Google Scholar
• Oku T, Yoshida M, Tomita G. Heat stability of the phototransforming activity of Chenopodium chlorophyll protein. Plant Cell Physiol. 1972;13:183–186.
   Web of Science ®Google Scholar
• Oku T, Yoshida M, Tomita G. The photoconversion of heat-treated Chenopodium chlorophyll protein and its pH dependence. Plant Cell Physiol. 1972;13:773–782.
   Web of Science ®Google Scholar
• Hagar WG, French CS. Energy transfer in chlorophyll protein 668: evidence for a stable electronic state involvement in its phototransformation. Carnegie Inst. Yearbook. 1974;73:706–716.
   Google Scholar
• Oku T, Tomita G. The photoconversion of heat-treated Chenopodium chlorophyll protein and its pH dependence. Plant Cell Physiol. 1975;16:1009–1016.
   Web of Science ®Google Scholar
• Hagar WG, Hiyama T. Characterization of the light-induced transient states of the chlorophyll proteins 668 and 743 from Atriplex rosea. Plant Physiol. 1979;63:1182–1186.10.1104/pp.63.6.1182
   PubMed Web of Science ®Google Scholar
• Noguchi T, Kamimura Y, Inoue Y, Itoh S. Photoconversion of a water-soluble chlorophyll protein from Chenopodium album: resonance Raman and Fourier transform infrared study of protein and pigment structures. Plant Cell Physiol. 1999;40:305–310.10.1093/oxfordjournals.pcp.a029542
   Web of Science ®Google Scholar
• Hirabayashi H, Amakawa M, Kamimura Y, Shino Y, Satoh H, Itoh S, Tamiaki H. Analysis of photooxidized pigments in water-soluble chlorophyll protein complex isolated from Chenopodium album. J. Photochem. Photobiol. 2006;183:121–125.10.1016/j.jphotochem.2006.03.003
   Web of Science ®Google Scholar
• Ohtsuki T, Ohshima S, Uchida A. Purification, crystallization and preliminary X-ray diffraction analysis of water-soluble chlorophyll-binding protein from Chenopodium album. Acta Crystallogr. Sect. F Strct. Biol. Csyst. Commun. 2007;63:740–741.10.1107/S1744309107035658
   PubMed Web of Science ®Google Scholar
• Takahashi S, Uchida A, Nakayama K, Satoh H. Three-step photoconversion of only three subunits of the water-soluble chlorophyll-binding protein tetramer from Chenopsodium album. Protein J. 2014;33:337–343.
   PubMed Web of Science ®Google Scholar
• Satoh H, Nakayama K, Okada M. Molecular cloning and functional expression of a water-soluble chlorophyll Protein, a putative carrier of chlorophyll molecules in cauliflower. J. Biol. Chem. 1998;273:30568–30575.10.1074/jbc.273.46.30568
   PubMed Web of Science ®Google Scholar
• Satoh H, Zanma A, Shinashi K. Molecular cloning and sequence analysis of a water-soluble chlorophyll protein cDNA from Japanese radish. J. Plant Physiol. 2002;159:325–327.10.1078/0176-1617-00704
   Web of Science ®Google Scholar
• Bektas I, Fellenberg C, Paulsen H. Water-soluble chlorophyll protein (WSCP) of Arabidopsis is expressed in the gynoecium and developing silique. Planta. 2012;236:251–259.10.1007/s00425-012-1609-y
   PubMed Web of Science ®Google Scholar
• Takahashi S, Yanai H, Nakamaru Y, Uchida A, Nakayama K, Satoh H. Molecular cloning, characterization and analysis of the intracellular localization of a water-soluble chl-binding protein from Brussels Sprouts (Brassica oleracea var. gemmifera). Plant Cell Physiol. 2012;53:879–891.10.1093/pcp/pcs031
   PubMed Web of Science ®Google Scholar
• Takahashi S, Ono M, Uchida A, Nakayama K, Satoh H. Molecular cloning and expression of a water-soluble chlorophyll-binding protein from Japanese wild radish. J. Plant Physiol. 2013;170:406–412.10.1016/j.jplph.2012.10.007
   PubMed Web of Science ®Google Scholar
• Takahashi S, Yanai H, Oka-Takayama Y, Zanma-Sohtome A, Fujiyama K, Uchida A, Nakayama K, Satoh H. Molecular cloning, characterization and analysis of the intracellular localization of a water-soluble chlorophyll-binding protein (WSCP) from Virginia pepperweed (Lepidium virginicum), a unique WSCP that preferentially binds chlorophyll b in vitro. Planta. 2013;238:1065–1080.10.1007/s00425-013-1952-7
   PubMed Web of Science ®Google Scholar
• Schmidt K, Fufezan C, Krieger-Liszkay A, Satoh H, Paulsen H. Recombinant water-soluble chlorophyll protein from Brassica oleracea var. Botrys binds various chlorophyll derivatives. Biochemistry. 2003;42:7427–7433.
   Google Scholar
• Hughes JL, Razeghifard R, Logue M, Oakley A, Wydrzynski T, Krausz E. Magneto-optic spectroscopy of a protein tetramer binding two exciton-coupled chlorophylls. J. Am. Chem. Soc. 2006;128:3649–3658.10.1021/ja056576b
   PubMed Web of Science ®Google Scholar
• Renger T, Trostmann I, Theiss C, Madjet ME, Richter M, Paulsen H, Eichler HJ, Knorr A, Renger G. Refinement of a structural model of a pigment−protein complex by accurate optical line shape theory and experiments. J. Phys. Chem. B. 2007;111:10487–10501.10.1021/jp0717241
   PubMed Web of Science ®Google Scholar
• Renger T, Madjet ME, Müh F, Trostmann I, Schmitt FJ, Theiss C, Paulsen H, Eichler HJ, Knorr A, Renger G. Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein. J. Phys. Chem. B. 2009;113:9948–9957.10.1021/jp901886w
   PubMed Web of Science ®Google Scholar
• Theiss C, Trostmann I, Andree S, Schmitt FJ, Renger T, Eichler HJ, Paulsen H, Renger G. Pigment−pigment and pigment−protein interactions in recombinant water-soluble chlorophyll proteins (WSCP) from cauliflower. J. Phys. Chem. B. 2007;111:13325–13335.10.1021/jp0723968
   PubMed Web of Science ®Google Scholar
• Schmitt FJ, Trostmann I, Theiss C, Pieper J, Renger T, Fuesers J, Hubrich EH, Paulsen H, Eichler HJ, Renger G. Excited state dynamics in recombinant water-soluble chlorophyll proteins (WSCP) from cauliflower investigated by transient fluorescence spectroscopy. J. Phys. Chem. B. 2008;112:13951–13961.10.1021/jp8024057
   PubMed Web of Science ®Google Scholar
• Pieper J, Rätsep M, Trostmann I, Paulsen H, Renger G, Freiberg A. Excitonic energy level structure and pigment−protein interactions in the recombinant water-soluble chlorophyll protein. I. Difference fluorescence line-narrowing. J. Phys. Chem. B. 2011;115:4042–4052.10.1021/jp111455g
   PubMed Web of Science ®Google Scholar
• Pieper J, Rätsep M, Trostmann I, Schmitt FJ, Theiss C, Paulsen H, Eichler HJ, Freiberg A, Renger G. Excitonic energy level structure and pigment−protein interactions in the recombinant water-soluble chlorophyll protein. II. Spectral hole-burning experiments. J. Phys. Chem. B. 2011;115:4053–4065.10.1021/jp111457t
   PubMed Web of Science ®Google Scholar
• Takahashi S, Uchida A, Nakayama K, Satoh H. The C-terminal extension peptide of non-photoconvertible water-soluble chlorophyll-binding proteins (Class II WSCPs) affects their solubility and stability: comparative analyses of the biochemical and chlorophyll-binding properties of recombinant Brassica, Raphanus and Lepidium WSCPs with or without their C-terminal extension peptides. Protein J. 2014;33:75–84.10.1007/s10930-013-9539-5
   PubMed Web of Science ®Google Scholar
• Takahashi S, Yoshikawa M, Kamada A, Ohtsuki T, Uchida A, Nakayama K, Satoh H. The photoconvertible water-soluble chlorophyll-binding protein of Chenopodium album is a member of DUF538, a superfamily that distributes in Embryophyta. J. Plant Physiol. 2013;170:1549–1552.10.1016/j.jplph.2013.06.001
   PubMed Web of Science ®Google Scholar
• Takahashi S, Seki Y, Uchida A, Nakayama K, and Satoh H, Cysteine-2 and Cys30 are essential for chlorophyll-binding activity of the water-soluble chlorophyll-binding protein (WSCP) of Chenopodium album. Biosci. Biotechnol. Biochem., doi:10.1080/09168451.2014.940274(in press).
   Web of Science ®Google Scholar
• Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic. Acids. Res. 1997;25:4876–4882.10.1093/nar/25.24.4876
   PubMed Web of Science ®Google Scholar
• Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987;4:406–425.
   PubMed Web of Science ®Google Scholar