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Originally published In Press as doi:10.1074/jbc.M411493200 on October 29, 2004
Originally published In Press as doi:10.1074/jbc.M411493200 on October 27, 2004
J. Biol. Chem., Vol. 280, Issue 1, 840-846, January 7, 2005
Anti-oxidative Stress System in Cyanobacteria
SIGNIFICANCE OF TYPE II PEROXIREDOXIN AND THE ROLE OF 1-Cys PEROXIREDOXIN IN SYNECHOCYSTIS SP. STRAIN PCC 6803*
Naomi Hosoya-Matsuda ,
Ken Motohashi ,
Hidehisa Yoshimura¶||,
Akiko Nozaki **,
Kazuhito Inoue**,
Masayuki Ohmori¶ , and
Toru Hisabori  
From the
Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259-R1-8, Midori-ku, Yokohama 226-8503, the ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 5800-3 Nagatsuta-cho, Midori-ku, Yokohama 226-0026, the ¶Department of Life Science, Graduate School of Arts and Sciences, University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, and the **Department of Biological Sciences, Kanagawa University, Hiratsuka, Kanagawa 259-1293, Japan
Two antioxidant proteins, SLL1621 and SLR1198, were captured in the cyanobacteria Synechocystis sp. PCC 6803 using thioredoxin affinity chromatography, which was first applied to the survey of thioredoxin target proteins in chloroplasts (
Motohashi, K., Kondoh, A., Stumpp, M. T., and Hisabori, T. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 11224-11229). They are annotated as AhpC/TSA family protein (SLL1621) and antioxidant protein (SLR1198) in CyanoBase (
Nakamura, Y., Kaneko, T., Hirosawa, M., Miyajima, N., and Tabata, S. (1998) Nucleic Acids Res. 26, 63-67). Based on sequence homology analysis SLL1621 and SLR1198 are categorized into type II peroxiredoxin and 1-Cys type peroxiredoxin, respectively. In vitro interaction between SLL1621 and thioredoxin was confirmed using the recombinant proteins expressed in Escherichia coli. Furthermore, we found that SLL1621 shows remarkable glutathione-dependent peroxidase activity. Disruption of the sll1621 gene had a dramatic effect on the viability of the cyanobacterial cells even under weak light conditions (50 µmol·m-2·s-1), suggesting this peroxiredoxin is essential for this cyanobacterium. In contrast, although the peroxidase activity of SLR1198 was scarcely detected, disruption of the gene, slr1198, certainly affected the growth rate of the cells. The results indicate the physiological significance of two different peroxiredoxins as an anti-oxidative stress system in cyanobacteria.
Received for publication, October 8, 2004
, and in revised form, October 22, 2004.
* This work was supported in part by the ATP System Project, Exploratory Research for Advanced Technology funded by the Japan Science and Technology Agency.
|| Present address: Center of Systems Biology and Ecology, Faculty of Science, Toho University, Funabashi, 274-8510 Chiba, Japan.
 Present address: Dept. of Biochemistry Molecular Biology, Faculty of Science, Saitama University, 255 Shimo-Ohkubo, Saitama, 338-8570 Saitama, Japan.
 To whom correspondence should be addressed. Tel.: 81-45-924-5234; Fax: 81-45-924-5277; E-mail: thisabor{at}res.titech.ac.jp.

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