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Plant and Cell Physiology, 2003, Vol. 44, No. 4 451-456
© 2003 Oxford University Press

Short Communications

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

Takahiro Henmi1, Hitoshi Yamasaki1, Shinsuke Sakuma1, Yuka Tomokawa1, Noriaki Tamura2, Jian-Ren Shen3 and Yasusi Yamamoto1,4

1 Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan
2 Department of Human Environmental Science, Fukuoka Women’s University, Fukuoka, 813-8529 Japan
3 RIKEN Harima Institute, Mikazuki-cho, Sayo-gun, Hyogo, 679-5148 Japan

Abstract

During the donor-side photoinhibition of spinach photosystem II, the reaction center D1 protein cross-linked with the antenna chlorophyll binding protein CP43 of photosystem II lacking the oxygen-evolving complex (OEC) subunit proteins. The cross-linking did not occur upon illumination of photosystem II samples that retained the OEC33, nor when OEC33-depleted photosystem II samples were reconstituted with the OEC33 prior to illumination. These results suggest that the D1 protein, CP43 and the OEC33 are located in close proximity at the lumenal side of photosystem II, and that the OEC33 suppresses the unnecessary contact between the D1 protein and CP43. Previously we presented data showing the D1 protein located adjacent to CP43 on the stromal side of photosystem II [Ishikawa et al. (1999) Biochim. Biophys. Acta 1413: 147]. The present data suggest that the spatial arrangement of the D1 protein and CP43 at the lumenal side of photosystem II in spinach chloroplasts is similar to that at the stromal side of photosystem II and is consistent with the assignment of these proteins recently proposed on the crystal structures of the photosystem II complexes from cyanobacteria [Zouni et al. (2001) Nature 409: 739, Kamiya and Shen 2003 Proc. Natl. Acad. Sci. USA, 100: 98]. Moreover, the data suggest that the binding condition and positioning of the OEC33 in the photosystem II complex from higher plants may be different from those in cyanobacteria.

Footnotes

4 Corresponding author: E-mail, yasusiya{at}cc.okayama-u.ac.jp; Fax, +81-86-251-7876.


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T. Henmi, M. Miyao, and Y. Yamamoto
Release and Reactive-Oxygen-Mediated Damage of the Oxygen-Evolving Complex Subunits of PSII during Photoinhibition
Plant Cell Physiol., February 15, 2004; 45(2): 243 - 250.
[Abstract] [Full Text] [PDF]


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