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Plant and Cell Physiology, 1990, Vol. 31, No. 4 479-488
© 1990

Article

Immunological Cross-Reactivity among Corresponding Proteins of Photosystems I and II from Widely Divergent Photosynthetic Organisms

Yasuhiro Kashino1, Isao Enami2, Kazuhiko Satoh1 and Sakae Katoh

1Department of Biology, Faculty of Science, University of Tokyo Hongo, Tokyo, 113 Japan
2Department of Biology, Faculty of Science, Science University of Tokyo Kagurazaka, Tokyo, 162 Japan

Immunological cross-reactivity among corresponding proteins associated with photosystems I and II in higher plants, green algae, red algae and cyanobacteria were examined with antisera raised against the proteins from Synechococcus elongatus and spinach. (1) Generally, the cross-reactivity was very high between closely related species but decreased with increasing phylogenetic distances between organisms. Exceptionally, proteins from red algae showed lower reactivities with the antisera against the cyanobacterial proteins than did corresponding proteins from green algae and higher plants. (2) The extent of the cross-reactivity was found to vary with the antisera used. Three antisera prepared against large chlorophyll-carrying proteins of photosystem I and photosystem II reaction center complexes of Synechococcus reacted with the corresponding proteins of all the organisms examined. By contrast, an antiserum raised against the extrinsic 35 kDa protein of the cyanobacterium reacted with none of corresponding 33 kDa proteins of other species. The antiserum against the spinach 33 kDa protein showed a wider range of cross-reactivity. Antisera raised against the Dl and D2 proteins from spinach were highly reactive with corresponding proteins from other photosynthetic organisms, whereas an antiserum against a well-conserved sequence of the spinach D2 protein showed limited cross-reactivity. The results show that, although the extent of immunological cross-reactivity is determined mainly by the homology between proteins, caution is indicated in the application of immunological methods to determinations of the distribution of various proteins related to photosystems I and II in very different organisms.

(Received December 8, 1989; Accepted March 12, 1990)
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