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 Henmi, Hitoshi Yamasaki, Shinsuke Sakuma, Yuka Tomokawa, Noriaki Tamura, Jian-Ren Shen, Yasusi Yamamoto

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)451-456
Number of pages6
JournalPlant and Cell Physiology
Volume44
Issue number4
DOIs
Publication statusPublished - Apr 1 2003
Externally publishedYes

Fingerprint

D1 protein
Photosystem II Protein Complex
Spinacia oleracea
photoinhibition
Chloroplasts
crosslinking
spinach
photosystem II
chloroplasts
Light
Proteins
proteins
Cyanobacteria
Lighting
lighting
Chlorophyll Binding Proteins
oxygen evolving complex
spatial data
Protein Subunits
protein subunits

Keywords

  • CP43
  • D1 protein
  • OEC33
  • Photosystem II
  • Protein cross-linking

ASJC Scopus subject areas

  • Plant Science
  • Physiology
  • Cell Biology

Cite this

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. / Henmi, Takahiro; Yamasaki, Hitoshi; Sakuma, Shinsuke; Tomokawa, Yuka; Tamura, Noriaki; Shen, Jian-Ren; Yamamoto, Yasusi.

In: Plant and Cell Physiology, Vol. 44, No. 4, 01.04.2003, p. 451-456.

Research output: Contribution to journalArticle

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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.",
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