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J. Biol. Chem., Vol. 280, Issue 26, 25277-25283, July 1, 2005

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Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana^*

Takahisa Ogawa, Yayoi Ueda, Kazuya Yoshimura, and Shigeru Shigeoka

From the Department of Advanced Bioscience, Faculty of Agriculture, Kinki University, 3327-204 Nakamachi, Nara 631-8505, Japan

Nudix hydrolases are a family of proteins that catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives. Twenty-four genes of the Nudix hydrolase homologues (AtNUDTs) with predicted localizations in the cytosol, chloroplasts, and mitochondria exist in Arabidopsis thaliana. Here, we demonstrated the comprehensive analysis of nine types of cytosolic AtNUDT proteins (AtNUDT1, -2, -4, -5, -6, -7, -9, -10, and -11). The recombinant proteins of AtNUDT2, -6, -7, and -10 showed both ADP-ribose and NADH pyrophosphatase activities with significantly high affinities compared with those of animal and yeast enzymes. The expression of each AtNUDT is individually regulated in different tissues. These findings suggest that most cytosolic AtNUDTs may substantially function in the sanitization of potentially hazardous ADP-ribose and the regulation of the cellular NADH/NAD⁺ ratio in plant cells. On the other hand, the AtNUDT1 protein had the ability to hydrolyze 8-oxo-dGTP with a K_m value of 6.8 µM and completely suppress the increased frequency of spontaneous mutations in the Escherichia coli mutT^- strain, indicating that AtNUDT1 is a functional homologue of E. coli MutT in A. thaliana and is involved in the prevention of spontaneous mutation. The results obtained here suggest that the plant Nudix family has evolved in a specific manner that differs from that of yeast and humans.

Received for publication, March 31, 2005 , and in revised form, April 25, 2005.

^* This work was supported by Grants-in-Aid for Scientific Research (15380078 to S. S.) from the Ministry of Education, Culture, Sports, Science, and Technology, Japan and from the Ministry of Agriculture, Forestry, and Fisheries, Japan (to S. S.). This work was also supported by the "Academic Frontier" Project for Private Universities: matching fund subsidy from Ministry of Education, Culture, Sports, Science and Technology, 2004-2008. 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.

Present address; Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan.

To whom correspondence should be addressed: Tel.: 81-742-43-8083; Fax: 81-742-43-8976; E-mail: shigeoka{at}nara.kindai.ac.jp.

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