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Plant and Cell Physiology, 1995, Vol. 36, No. 7 1169-1177
© 1995

Identification of the Carboxyl-Terminal Processing Protease for the D1 Precursor Protein of the Photosystem II Reaction Center of Spinach

Shuji Fujita1,3, Noritoshi Inagaki2, Yumiko Yamamoto1, Fumiko Taguchi1, Akira Matsumoto1,2 and Kimiyuki Satoh1,2

1 Department of Biology, Okayama University Okayama, 700 Japan
2 Division of Biological Regulation and Photobiology, National Institute for Basic Biology Okazaki, 444 Japan

The enzyme involved in the carboxyl-terminal processing of the D1 precursor protein (pD1) of the photosystem II reaction center was purified from extracts of sonicated spinach thylakoids by a method that included chromatography on quaternary aminoethyl anion-exchange, hydroxylapatite, copper-chelating affinity and gel-filtration columns. The enzyme was identified, from its chromatographic behavior, to be a monomeric protein of about 45 kDa. The sequence of the amino-terminal 27 amino acids of this protein was determined directly, which exhibited low but appreciable (37%) homology to that deduced from a gene (ctpA) in Synechocystis sp. PCC 6803 that was proposed recently to encode the processing protease from results of genetic complementation analysis.

3Present address: Asahi Kasei Chem. Co.

(Received June 1, 1995; Accepted July 7, 1995)
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