Cloning and Characterization of a New Member of the Nudix Hydrolases from Human and Mouse

Yang, Hanjing; Slupska, Malgorzata M.; Yue, Wei; Tai, J Y; Luther, Wendy M.; Xia, Yu‐Rong; Shih, Diana M.; Chiang, Ju‐Huei; Baikalov, Claudia; Fitz‐Gibbon, Sorel; Phan, Isabella T.; Conrad, Alexis; Miller, Jeffrey H

doi:10.1074/jbc.275.12.8844

Cited by 61 publications

(56 citation statements)

References 43 publications

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“…The recombinant proteins of AtNUDT2, -6, -7, and -10 hydrolyzed both ADP-ribose and NADH to AMP. These proteins showed a high affinity for ADP-ribose compared with the other ADP-ribose pyrophosphatases, hNUDT5 (25), M. jannaschii ADP-ribose pyrophosphatase, MJ1149 (23), and cyanobacterium Synechococcus sp. PCC 7002 ADP-ribose pyrophosphatase, NuhA (31) ( Table II).…”

Section: Resultsmentioning

confidence: 99%

“…Although it is yet to be proven, it is assumed that these enzymes play an important role in maintaining the concentration of intracellular ADP-ribose at a sub-toxic level, because the accumulation of ADP-ribose can be potentially cytotoxic due to its ability to modify protein and to bind to ATP-activated K ϩ channels (22). It has been demonstrated that the gene products from Methanococcus jannaschii MJ1149, E. coli orf186, and Saccharomyces cerevisiae YSA1, and the human and mouse Ysa1p homologues, NUDT5 and Nudt5, respectively, have activities toward ADP-ribose (3,(23)(24)(25).…”

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confidence: 99%

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Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana

Ogawa

Ueda

Yoshimura³

et al. 2005

Journal of Biological Chemistry

126

170

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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 M 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.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana

Ogawa

Ueda

Yoshimura³

et al. 2005

Journal of Biological Chemistry

126

170

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“…Group I consists of bacterial types of ADP-ribose pyrophosphatase, such as ADPRase in E. coli and MT-ADPRase in M. tuberculosis. Group II consists of eukaryotic types of ADPsugar pyrophosphatase, such as NUDT5 in humans and YSA1 in Saccharomyces cerevisiae, which hydrolyze ADP-sugars, including ADP-ribose, ADP-mannose, and ADP-glucose (33). Group III consists of archaeal types of ADP-ribose pyrophosphatase, such as MJ1149 in M. jannaschii and NuhA in Synechococcus sp.…”

Section: Selection Of Putative Adp-ribose Pyrophosphatasesmentioning

confidence: 99%

Systematic Characterization of the ADP-Ribose Pyrophosphatase Family in the Cyanobacterium Synechocystis sp. Strain PCC 6803

2005

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We have characterized four putative ADP-ribose pyrophosphatases Sll1054, Slr0920, Slr1134, and Slr1690 in the cyanobacterium Synechocystis sp. strain PCC 6803. Each of the recombinant proteins was overexpressed in Escherichia coli and purified. Sll1054 and Slr0920 hydrolyzed ADP-ribose specifically, while Slr1134 hydrolyzed not only ADP-ribose but also NADH and flavin adenine dinucleotide. By contrast, Slr1690 showed very low activity for ADP-ribose and had four substitutions of amino acids in the Nudix motif, indicating that Slr1690 is not an active ADP-ribose pyrophosphatase. However, the quadruple mutation of Slr1690, T73G/ I88E/K92E/A94G, which replaced the mutated amino acids with those conserved in the Nudix motif, resulted in a significant (6.1 ؋ 10 2 -fold) increase in the k cat value. These results suggest that Slr1690 might have evolved from an active ADP-ribose pyrophosphatase. Functional and clustering analyses suggested that Sll1054 is a bacterial type, while the other three and Slr0787, which was characterized previously (Raffaelli et al., FEBS Lett. 444:222-226, 1999), are phylogenetically diverse types that originated from an archaeal Nudix protein via molecular evolutionary mechanisms, such as domain fusion and amino acid substitution.

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“…For example, the enzymes with pyrophosphohydrolase activity hydrolyze oxidized nucleotides, 8-oxo-7,8-dihydro-2#-(deoxy)guanosine 5#-triphosphate [8-oxo-(d)GTP] from Escherichia coli and human (Maki and Sekiguchi, 1992;Furuichi et al, 1994), NADH from E. coli, Saccharomyces cerevisiae, and human (Frick and Bessman, 1995;Xu et al, 2000;AbdelRaheim et al, 2003), CoA from S. cerevisiae, mice, and Caenorhabditis elegans (Cartwright et al, 2000;Gasmi and McLennan, 2001;AbdelRaheim and McLennan, 2002), ADP-Rib from human, Methanococcus jannaschii, and Synechococcus PCC7002 (Sheikh et al, 1998;Yang et al, 2000;Okuda et al, 2004), and diadenosine polyphosphates (Ap n A; n = 4-5) from C. elegans and Thermus thermophilus (Abdelghany et al, 2001;Iwai et al, 2004). However, the physiological functions of these subfamilies are still unclear, although some characteristics in vivo, such as subcellular distribution, have been determined (Cartwright et al, 2000;AbdelRaheim et al, 2001AbdelRaheim et al, , 2003Gasmi and McLennan, 2001).…”

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Molecular Characterization of Organelle-Type Nudix Hydrolases in Arabidopsis

et al. 2008

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Nudix (for nucleoside diphosphates linked to some moiety X) hydrolases act to hydrolyze ribonucleoside and deoxyribonucleoside triphosphates, nucleotide sugars, coenzymes, or dinucleoside polyphosphates. Arabidopsis (Arabidopsis thaliana) contains 27 genes encoding Nudix hydrolase homologues (AtNUDX1 to -27) with a predicted distribution in the cytosol, mitochondria, and chloroplasts. Previously, cytosolic Nudix hydrolases (AtNUDX1 to -11 and -25) were characterized. Here, we conducted a characterization of organelle-type AtNUDX proteins (AtNUDX12 to -24, -26, and -27). AtNUDX14 showed pyrophosphohydrolase activity toward both ADP-ribose and ADP-glucose, although its K m value was approximately 100-fold lower for ADP-ribose (13.0 6 0.7 mM) than for ADP-glucose (1,235 6 65 mM). AtNUDX15 hydrolyzed not only reduced coenzyme A (118.7 6 3.4 mM) but also a wide range of its derivatives. AtNUDX19 showed pyrophosphohydrolase activity toward both NADH (335.3 6 5.4 mM) and NADPH (36.9 6 3.5 mM). AtNUDX23 had flavin adenine dinucleotide pyrophosphohydrolase activity (9.1 6 0.9 mM). Both AtNUDX26 and AtNUDX27 hydrolyzed diadenosine polyphosphates (n = 4-5). A confocal microscopic analysis using a green fluorescent protein fusion protein showed that AtNUDX15 is distributed in mitochondria and AtNUDX14 -19, -23, -26, and -27 are distributed in chloroplasts. These AtNUDX mRNAs were detected ubiquitously in various Arabidopsis tissues. The T-DNA insertion mutants of AtNUDX13,, and -27 did not exhibit any phenotypical differences under normal growth conditions. These results suggest that Nudix hydrolases in Arabidopsis control a variety of metabolites and are pertinent to a wide range of physiological processes.

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Cloning and Characterization of a New Member of the Nudix Hydrolases from Human and Mouse

Cited by 61 publications

References 43 publications

Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana

Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana

Systematic Characterization of the ADP-Ribose Pyrophosphatase Family in the Cyanobacterium Synechocystis sp. Strain PCC 6803

Molecular Characterization of Organelle-Type Nudix Hydrolases in Arabidopsis

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