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J. Biol. Chem., Vol. 280, Issue 36, 31595-31602, September 9, 2005

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Photosystem II Assembly in CP47 Mutant of Synechocystis sp. PCC 6803 Is Dependent on the Level of Chlorophyll Precursors Regulated by Ferrochelatase^*

Roman Sobotka¶, Josef Komenda, Ladislav Bumba||, and Martin Tichy

From the Institute of Physical Biology, University of South Bohemia, 373 33 Nove Hrady, the Department of Autotrophic Microorganisms, Institute of Microbiology, Opatovicky mlyn, 379 71 Trebon, and the ^||Institute of Plant Molecular Biology, Branisovska 31, 370 05 Ceske Budejovice, Czech Republic

Accumulation of chlorophyll and expression of the chlorophyll (Chl)-binding CP47 protein that serves as the core antenna of photosystem II are indispensable for the assembly of a functional photosystem II. We have characterized the CP47 mutant with an impaired photosystem II assembly and its two spontaneous pseudorevertants with their much improved photoautotrophic growth. The complementing mutations in these pseudorevertants were previously mapped to the ferrochelatase gene (1). We demonstrated that complementing mutations dramatically decrease ferrochelatase activity in pseudorevertants and that this decrease is responsible for their improved photoautotrophic growth. Photoautotrophic growth of the CP47 mutant was also restored by in vivo inhibition of ferrochelatase by a specific inhibitor. The decrease in ferrochelatase activity in pseudorevertants was followed by increased steady-state levels of Chl precursors and Chl, leading to CP47 accumulation and photosystem II assembly. Similarly, supplementation of the CP47 mutant with the Chl precursor Mg-protoporphyrin IX increased the number of active photosystem-II centers, suggesting that synthesis of the mutated CP47 protein is enhanced by an increased Chl availability in the cell. The probable role of ferrochelatase in the regulation of Chl biosynthesis is discussed.

Received for publication, June 1, 2005 , and in revised form, July 14, 2005.

^* This work was supported by the Grant Agency of the Czech Academy of Sciences (Project B5817301 to R. S.), by Institutional Research Concept AV0Z50200510 (to J. K. and M. T.), and by the Ministry of Education, Youth and Sports (Project MSM6007665808 to J. K. and M. T). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2 and Table S1.

^¶ To whom correspondence should be addressed: Tel.: 420-384-722-268; Fax: 420-384-721-246; E-mail: sobotka{at}alga.cz.

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