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Assay of Photoinhibition and Heat Inhibition of Photosystem II in Higher Plants

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Photosynthesis Research Protocols

Part of the book series: Methods in Molecular Biology ((MIMB,volume 684))

Abstract

When thylakoids of higher plant chloroplasts are exposed to excessive light or moderate heat stress, photosystem II reaction center-binding protein D1 is damaged. The photodamage of the D1 protein is caused by reactive oxygen species, mostly singlet oxygen, and also by endogenous cationic radicals generated by the photochemical reactions of photosystem II. Moreover, it was shown recently that the damage to the D1 protein by moderate heat stress is due to reactive oxygen species produced by lipid peroxidation near photosystem II. To maintain photosystem II activity, the oxidatively damaged D1 protein must be replaced by a newly synthesized copy, and thus degradation and removal of the photo- or heat-damaged D1 protein are essential for maintaining the viability of photosystem II. In this chapter, we describe the methods for assaying photoinhibition and heat inhibition of photosystem II in higher plant materials.

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References

  1. Macpherson, A. N., Telfer, A., Barber, J., and Truscott, T. G. (1993) Direct detection of singlet oxygen from isolated Photosystem II reaction centres. Biochim Biophys Acta 1143, 301–309.

    Article  CAS  Google Scholar 

  2. Hideg, É, Spetea, C., and Vass, I. (1994) Singlet oxygen production in thylakoid membranes during photoinhibition as detected by EPR spectroscopy. Photosynth Res 39, 191–199.

    Article  CAS  Google Scholar 

  3. Mishra, N. P., Francke, C., van Gorkom, H. J., and Ghanotakis, D. F. (1994) Destructive role of singlet oxygen during aerobic illumination of the photosystem II core complex. Biochim Biophys Acta 1186, 81–90.

    Article  CAS  Google Scholar 

  4. Barber, J. and Andersson, B. (1992) Too much of a good thing: light can be bad for photosynthesis. Trends Biochem Sci 17, 61–66.

    Article  PubMed  CAS  Google Scholar 

  5. Aro, E.-M., Virgin, I., and Andersson, B. (1993) Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim Biophys Acta 1143, 113–134.

    Article  PubMed  CAS  Google Scholar 

  6. Yamamoto, Y. (2001) Quality control of photosystem II. Plant Cell Physiol 42, 121–128.

    Article  PubMed  CAS  Google Scholar 

  7. Yamamoto, Y., Aminaka, R., Yoshioka, M., Khatoon, M., Komayama, K., Takenaka, D., Yamashita, A., Nijo, N., Inagawa, K., Morita, N., Sasaki, T., and Yamamoto, Y. (2008) Quality control of photosystem II: impact of light and heat stresses. Photosynth Res 98, 589–608.

    Article  PubMed  CAS  Google Scholar 

  8. Greenberg, B. M., Gaba, V., Mattoo, A. K., and Edelman, M. (1987) Identification of a primary in vivo degradation product of the rapidly-turning-over 32 kd protein of photosystem II. EMBO J 6, 2865–2869.

    PubMed  CAS  Google Scholar 

  9. Andersson, B. and Aro, E.-M. (1997) Proteolytic activities and proteases of plant chloroplasts. Physiol Plant 100, 780–793.

    Article  CAS  Google Scholar 

  10. Ishikawa, Y., Nakatani, E., Henmi, T., Ferjani, A., Harada, Y., Tamura, N., and Yamamoto, Y. (1999) Turnover of the aggregates and cross-linked products of the D1 protein generated by acceptor-side photoinhibition of photosystem II. Biochim Biophys Acta 1413, 147–158.

    Article  PubMed  CAS  Google Scholar 

  11. Yamamoto, Y. and Akasaka, T. (1995) Degradation of antenna chlorophyll-binding protein CP43 during photoinhibition of photosystem II. Biochemistry 34, 9038–9045.

    Article  PubMed  CAS  Google Scholar 

  12. De Las Rivas, J., Andersson, B., and Barber, J. (1992) Two sites of primary degradation of the D1-protein induced by acceptor or donor side photo-inhibition in photosystem II core complexes. FEBS Lett 301, 246–252.

    Article  PubMed  Google Scholar 

  13. Henmi, T., Yamasaki, H., Sakuma, S., Tomokawa, Y., Tamura, N., Shen, J.-R., and Yamamoto, Y. (2003) Dynamic interaction between the D1 protein, CP43 and OEC33 at the lumenal side of photosystem II in spinach chloroplasts: evidence from light-induced cross-linking of the proteins in the donor-side photoinhibition. Plant Cell Physiol 44, 451–456.

    Article  PubMed  CAS  Google Scholar 

  14. Yoshioka, M., Uchida, S., Mori, H., Komayama, K., Ohira, S., Morita, N., Nakanishi, T., and Yamamoto, Y. (2006) Quality control of photosystem II: cleavage of reaction center D1 protein in spinach thylakoids by FtsH protease under moderate heat stress. J Biol Chem 281, 21660–21669.

    Article  PubMed  CAS  Google Scholar 

  15. Yamashita, A., Nijo, N., Pospíšil, P., Morita, N., Takenaka, D., Aminaka, R., Yamamoto, Y., and Yamamoto, Y. (2008) Quality control of photosystem II: reactive oxygen species are responsible for the damage to photosystem II under moderate heat stress. J Biol Chem 283, 28380–28391.

    Article  PubMed  CAS  Google Scholar 

  16. Norén, H., Svensson, P., and Andersson, B. (2004) A convenient and versatile hydroponic cultivation system for Arabidopsis thaliana. Physiol Plant 121, 343–348.

    Article  Google Scholar 

  17. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.

    Article  PubMed  CAS  Google Scholar 

  18. Ikeuchi, M. and Inoue, Y. (1988) A new 4.8-kDa polypeptide intrinsic to the PSII reaction center, as revealed by modified SDS-PAGE with improved resolution of low-molecular-weight proteins. Plant Cell Physiol 29, 1233–1239.

    CAS  Google Scholar 

  19. Sokolenko, A., Altschmied, L., and Herrmann, R. G. (1997) Sodium dodecyl sulfate-stable proteases in chloroplasts. Plant Physiol 115, 827–832.

    PubMed  CAS  Google Scholar 

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Correspondence to Yasusi Yamamoto .

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Nijo, N., Lundin, B., Yoshioka, M., Morita, N., Yamamoto, Y. (2011). Assay of Photoinhibition and Heat Inhibition of Photosystem II in Higher Plants. In: Carpentier, R. (eds) Photosynthesis Research Protocols. Methods in Molecular Biology, vol 684. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-925-3_17

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  • DOI: https://doi.org/10.1007/978-1-60761-925-3_17

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-60761-924-6

  • Online ISBN: 978-1-60761-925-3

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