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Ikeuchi M, Plumley FG, Inoue Y, et al. Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant Physiol. 1987;85(3):638-42doi: 10.1104/pp.85.3.638.
Ikeuchi, M., Plumley, F. G., Inoue, Y., & Schmidt, G. W. (1987). Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant physiology, 85(3), 638-42. https://doi.org/10.1104/pp.85.3.638
Ikeuchi, M, et al. "Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants." Plant physiology vol. 85,3 (1987): 638-42. doi: https://doi.org/10.1104/pp.85.3.638
Ikeuchi M, Plumley FG, Inoue Y, Schmidt GW. Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant Physiol. 1987 Nov;85(3):638-42. doi: 10.1104/pp.85.3.638. PMID: 16665752; PMCID: PMC1054314.
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Plant Physiol. 1987 Nov;85(3):638-42. doi: 10.1104/pp.85.3.638.

Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants.

Plant physiology

M Ikeuchi, F G Plumley, Y Inoue, G W Schmidt

Affiliations

  1. Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan.

PMID: 16665752 PMCID: PMC1054314 DOI: 10.1104/pp.85.3.638

Abstract

Phosphorylated thylakoid proteins of spinach (Spinacia oleracea L.) and pea (Pisum sativum L.) were solubilized, fractionated by sucrose density gradient centrifugation, and analyzed by gel electrophoresis and crossed immunoelectrophoresis to identify the phosphoproteins. It was found that in addition to intense phosphorylation of light-harvesting chlorophyll complex II, four photosystem II components, CP43 apoprotein, D1, D2, and a 10 to 11 kilodalton protein, are substantially phosphorylated in the light. Furthermore, the CP43 apoprotein, D1 and D2 can be resolved into two electrophoretic subspecies, only one of which is phosphorylated. This indicates that only a fraction of the PSII polypeptides is phosphorylated. Finally, analysis of detergent procedures suggests that the 10 to 11 kilodalton phosphoprotein is a peripheral component of the O(2)-evolving PSII reaction center complex.

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