Cross-Linking Studies on the Membrane Topography of Photosystem I Reaction Center Complex in Synechococcus sp.
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概要
- 論文の詳細を見る
The subunit arrangement of the photosystem I reaction center complex in the thylakoid membranes of the thermophilic cyanobacterium Synechococcus sp. was examined using three cross-linking reagents. (1) Treatments of osmotically shocked and NaBr-washed protoplasts with low concentrations of hydrophilic cross-linking reagents, dimethyladipimidate and glutaraldehyde, preferentially decreased 62, 60, 14 and 13 kDa polypeptides of the photosystem I reaction center complex resolved by SDS-polyacrylamide gel electrophoresis, together with the anchor protein and allophycocyanin which are associated with the outer surface of the thylakoid membranes. This suggests that these four subunits of the photosystem I complex are exposed on the stromal surface of thylakoid membranes. In contrast, a hydrophobic cross-linker, hexamethylenediisocyanate, unspecifically cross-linked most of the membrane polypeptides. (2) The 13 and 14 kDa polypeptides decreased always in parallel to each other on treatment of the protoplasts or isolatd CP1-a with the three cross-linking reagents, and the disappearance of the two polypeptides was accompanied by the appearance of a cross-linked product(s), when fixed with glutaraldehyde and hexamethylenediisocyanate. The results suggest that the 13 and 14 kDa polypeptides are neighboring polypeptides in the complex.
- 日本植物生理学会の論文
著者
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Enami Isao
Department of Biology, Faculty of Science, Science University of Tokyo
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Enami Isao
Department Of Biology Faculty Of Science Science University Of Tokyo
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OHTA Hisataka
Department of Biology, Faculty of Science, Tokyo University of Science
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Ohta Hisataka
Department Of Biology Faculty Of Science Science University Of Tokyo
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Miyaoka Takeshi
Department of Biology, Faculty of Science, Science University of Tokyo
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Miyaoka Takeshi
Department Of Biology Faculty Of Science Science University Of Tokyo
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