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. 1995 Mar;107(3):943–952. doi: 10.1104/pp.107.3.943

Photosystem II Regulation and Dynamics of the Chloroplast D1 Protein in Arabidopsis Leaves during Photosynthesis and Photoinhibition.

A W Russell 1, C Critchley 1, S A Robinson 1, L A Franklin 1, GGR Seaton 1, W S Chow 1, J M Anderson 1, C B Osmond 1
PMCID: PMC157211  PMID: 12228414

Abstract

Arabidopsis thaliana leaves were examined in short-term (1 h) and long-term (10 h) irradiance experiments involving growth, saturating and excess light. Changes in photosynthetic and chlorophyll fluorescence parameters and in populations of functional photosystem II (PSII) centers were independently measured. Xanthophyll pigments, 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU)-binding sites, the amounts of D1 protein, and the rates of D1 protein synthesis were determined. These comprehensive studies revealed that under growth or light-saturating conditions, photosynthetic parameters remained largely unaltered. Photoprotection occurred at light saturation indicated by a dark-reversible increase in non-photochemical quenching accompanied by a 5-fold increase in antheraxanthin and zeaxanthin. No consistent change in the concentrations of functional PSII centers, DCMU-binding sites, or D1 protein pool size occurred. D1 protein synthesis was rapid. In excess irradiance, quantum yield of O2 evolution and the efficiency of PSII were reduced, associated with a 15- to 20-fold increase in antheraxanthin and zeaxanthin and a sustained increase in nonphotochemical quenching. A decrease in functional PSII center concentration occurred, followed by a decline in the concentration of D1 protein; the latter, however, was not matched by a decrease in DCMU-binding sites. In the most extreme treatments, DCMU-binding site concentration remained 2 times greater than the concentration of D1 protein recognized by antibodies. D1 protein synthesis rates remained unaltered at excess irradiances.

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Selected References

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  1. Aro E. M., McCaffery S., Anderson J. M. Photoinhibition and D1 Protein Degradation in Peas Acclimated to Different Growth Irradiances. Plant Physiol. 1993 Nov;103(3):835–843. doi: 10.1104/pp.103.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aro E. M., Virgin I., Andersson B. Photoinhibition of Photosystem II. Inactivation, protein damage and turnover. Biochim Biophys Acta. 1993 Jul 5;1143(2):113–134. doi: 10.1016/0005-2728(93)90134-2. [DOI] [PubMed] [Google Scholar]
  3. Barber J., Andersson B. Too much of a good thing: light can be bad for photosynthesis. Trends Biochem Sci. 1992 Feb;17(2):61–66. doi: 10.1016/0968-0004(92)90503-2. [DOI] [PubMed] [Google Scholar]
  4. De Las Rivas J., Shipton C. A., Ponticos M., Barber J. Acceptor side mechanism of photoinduced proteolysis of the D1 protein in photosystem II reaction centers. Biochemistry. 1993 Jul 13;32(27):6944–6950. doi: 10.1021/bi00078a019. [DOI] [PubMed] [Google Scholar]
  5. Demmig B., Winter K., Krüger A., Czygan F. C. Photoinhibition and zeaxanthin formation in intact leaves : a possible role of the xanthophyll cycle in the dissipation of excess light energy. Plant Physiol. 1987 Jun;84(2):218–224. doi: 10.1104/pp.84.2.218. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kuhlman P. A., Hemmings L., Critchley D. R. The identification and characterisation of an actin-binding site in alpha-actinin by mutagenesis. FEBS Lett. 1992 Jun 15;304(2-3):201–206. doi: 10.1016/0014-5793(92)80619-r. [DOI] [PubMed] [Google Scholar]
  7. Kyle D. J., Ohad I., Arntzen C. J. Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes. Proc Natl Acad Sci U S A. 1984 Jul;81(13):4070–4074. doi: 10.1073/pnas.81.13.4070. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ruban A. V., Young A. J., Horton P. Induction of Nonphotochemical Energy Dissipation and Absorbance Changes in Leaves (Evidence for Changes in the State of the Light-Harvesting System of Photosystem II in Vivo). Plant Physiol. 1993 Jul;102(3):741–750. doi: 10.1104/pp.102.3.741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Shipton C. A., Barber J. In vivo and in vitro photoinhibition reactions generate similar degradation fragments of D1 and D2 photosystem-II reaction-centre proteins. Eur J Biochem. 1994 Mar 15;220(3):801–808. doi: 10.1111/j.1432-1033.1994.tb18682.x. [DOI] [PubMed] [Google Scholar]
  10. Shipton C. A., Barber J. Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6691–6695. doi: 10.1073/pnas.88.15.6691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Sundby C., Chow W. S., Anderson J. M. Effects on Photosystem II Function, Photoinhibition, and Plant Performance of the Spontaneous Mutation of Serine-264 in the Photosystem II Reaction Center D1 Protein in Triazine-Resistant Brassica napus L. Plant Physiol. 1993 Sep;103(1):105–113. doi: 10.1104/pp.103.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Sundby C., McCaffery S., Anderson J. M. Turnover of the photosystem II D1 protein in higher plants under photoinhibitory and nonphotoinhibitory irradiance. J Biol Chem. 1993 Dec 5;268(34):25476–25482. [PubMed] [Google Scholar]
  13. Tischer W., Strotmann H. Relationship between inhibitor binding by chloroplasts and inhibition of photosynthetic electron transport. Biochim Biophys Acta. 1977 Apr 11;460(1):113–125. doi: 10.1016/0005-2728(77)90157-8. [DOI] [PubMed] [Google Scholar]

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