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J. Biol. Chem., Vol. 281, Issue 31, 21660-21669, August 4, 2006

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Quality Control of Photosystem II

CLEAVAGE OF REACTION CENTER D1 PROTEIN IN SPINACH THYLAKOIDS BY FtsH PROTEASE UNDER MODERATE HEAT STRESS^*

Miho Yoshioka, Suguru Uchida, Hiroki Mori, Keisuke Komayama, Satoshi Ohira, Noriko Morita, Tohru Nakanishi, and Yasusi Yamamoto¹

From the Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530 and the School of Pharmacy, Shujitsu University, Okayama 703-8516, Japan

When spinach thylakoids were subjected to moderate heat stress (40 °C for 30 min), oxygen evolution was inhibited, and cleavage of the reaction center-binding protein D1 of photosystem II took place, producing 23-kDa N-terminal fragments. The D1 cleavage was greatly facilitated by the addition of 0.15 mM ZnCl₂ and 1 mM ATP and was completely inhibited by 1 mM EDTA, indicating the participation of an ATP-dependent metalloprotease(s) in the D1 cleavage. Herbicides 3-(3,4-dichlorophenyl)-1,1-dimethyl urea, bromoxynil, and ioxynil, all of which bind to the Q_B site, inhibited the D1 cleavage, suggesting that the DE-loop of the D1 protein is the heat-sensitive cleavage site. We solubilized the protease by treating the thylakoids with 2 M KSCN and detected a protease activity in the supernatant by gelatin activity gel electrophoresis in the 70–80-kDa region. The antibodies against tobacco FtsH and Arabidopsis FtsH2 reacted with a 70–80-kDa band of the KSCN-solubilized fraction, which suggests the presence of FtsH in the fraction. In accordance with this finding, we identified the homolog to Arabidopsis FtsH8 in the 70–80-kDa region by matrix-assisted laser desorption ionization time-of-flight mass analysis of the thylakoids. The KSCN-solubilized fraction was successively reconstituted with thylakoids to show heat-induced cleavage of the D1 protein and production of the D1 fragment. These results strongly suggest that an FtsH protease(s) is involved in the primary cleavage of the D1 protein under moderate heat stress.

Received for publication, March 28, 2006

^* This work was supported in part by grants from the Ministry of Education, Culture, Science, Sports and Technology, Japan, the Yamada Science Foundation, the Wesco Science Promotion Foundation, and by Excellent Research Project Grant of Okayama University. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 81-86-251-7860; Fax: 81-86-251-7876; E-mail: yasusiya{at}cc.okayama-u.ac.jp.

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