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Plant and Cell Physiology, 1982, Vol. 23, No. 4 663-667
© 1982

Article

Evidence against Identity of the Atrazine Receptor Protein with the 33-Kilodalton Protein from Spinach Chloroplasts

Tomohiko Kuwabara1 and Norio Murata2

Department of Biology, University of Tokyo Komaba, Meguro-ku, Tokyo 153, Japan

2To whom correspondence and reprint requests should be addressed

To evaluate the capacity of binding between the 33-kdalton protein and atrazine, we investigated the effect of the 33-kdalton protein on the inhibitory action of atrazine in spinach chloroplasts. The sensitivity of the Hill reaction with ferricyanide to atrazine was not affected at all by the added 33-kdalton protein. This fact suggests that the 33-kdalton protein is incapable of binding atrazine. In photosystem II particles defective in 33-kdalton protein, on the other hand, atrazine effectively inhibited the electron transport reaction from diphenylcarbazide to dichlorophenol indophenol. After the particles were treated with trypsin to eliminate the polypeptides having molecular masses of 34, 44 and 48 kdaltons, the electron transport reaction became markedly insensitive to atrazine. These findings indicate that the 33-kdalton protein is different from the atrazine receptor protein.

1 Present address: Department of Chemistry, Faculty of Science, Toho University, Miyama 2-2-1, Funabashi, Chiba 274, Japan.

(Received January 28, 1982; Accepted April 12, 1982)
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