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. 1987 Nov;85(3):638–642. 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 1

Masahiko Ikeuchi 1,2, F Gerald Plumley 1,2, Yorinao Inoue 1,2, Gregory W Schmidt 1,2
PMCID: PMC1054314  PMID: 16665752

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 O2-evolving PSII reaction center complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chua N. H., Bennoun P. Thylakoid membrane polypeptides of Chlamydomonas reinhardtii: wild-type and mutant strains deficient in photosystem II reaction center. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2175–2179. doi: 10.1073/pnas.72.6.2175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Coughlan S. J., Hind G. Purification and characterization of a membrane-bound protein kinase from spinach thylakoids. J Biol Chem. 1986 Aug 25;261(24):11378–11385. [PubMed] [Google Scholar]
  3. Delepelaire P. Partial characterization of the biosynthesis and integration of the Photosystem II reaction centers in the thylakoid membrane of Chlamydomonas reinhardtii. EMBO J. 1984 Apr;3(4):701–706. doi: 10.1002/j.1460-2075.1984.tb01872.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Farchaus J., Dilley R. A. Purification and partial sequence of the Mr 10,000 phosphoprotein from spinach thylakoids. Arch Biochem Biophys. 1986 Jan;244(1):94–101. doi: 10.1016/0003-9861(86)90097-4. [DOI] [PubMed] [Google Scholar]
  5. Plumley F. G., Schmidt G. W. Rocket and crossed immunoelectrophoresis of proteins solubilized with sodium dodecyl sulfate. Anal Biochem. 1983 Oct 1;134(1):86–95. doi: 10.1016/0003-2697(83)90267-1. [DOI] [PubMed] [Google Scholar]
  6. Steinback K. E., Bose S., Kyle D. J. Phosphorylation of the light-harvesting chlorophyll-protein regulates excitation energy distribution between photosystem II and photosystem I. Arch Biochem Biophys. 1982 Jun;216(1):356–361. doi: 10.1016/0003-9861(82)90221-1. [DOI] [PubMed] [Google Scholar]
  7. Westhoff P., Farchaus J. W., Herrmann R. G. The gene for the Mr 10,000 phosphoprotein associated with photosystem II is part of the psbB operon of the spinach plastid chromosome. Curr Genet. 1986;11(3):165–169. doi: 10.1007/BF00420602. [DOI] [PubMed] [Google Scholar]
  8. Widger W. R., Farchaus J. W., Cramer W. A., Dilley R. A. Studies on the relation of the Mr 9000 phosphoprotein to cytochrome b-559 in spinach thylakoid membranes. Arch Biochem Biophys. 1984 Aug 15;233(1):72–79. doi: 10.1016/0003-9861(84)90602-7. [DOI] [PubMed] [Google Scholar]

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