Cloning and Characterization of the First Member of the Nudix Family from Arabidopsis thaliana

Dobrzanska, Marta; Szurmak, Blanka; Wysłouch‐Cieszyńska, Aleksandra; Kraszewska, Elzbieta

doi:10.1074/jbc.m205207200

Cited by 27 publications

(33 citation statements)

References 43 publications

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“…AtNUDT1 was previously reported to have activity toward NADH in the presence of 5 mM Mn 2ϩ (20). However, this activity was not detected in the presence of 5 mM Mg 2ϩ (Table I).…”

Section: Resultsmentioning

confidence: 70%

“…1). Among them, only AtNUDT1 has been characterized as an NADH, dihydroneopterin triphosphate, and (deoxy)nucleoside triphosphate pyrophosphatases (20,21). The deduced amino acid sequences of AtNUDTs showed low homology (11.6 -25.9%) with those of E. coli MutT and human MTH1, and their sizes ranged from 16.4 kDa (147 amino acids) to 86.9 kDa (772 amino acids).…”

Section: Resultsmentioning

confidence: 99%

“…Based on a BLAST search (19) of the DNA data base, it is likely that 24 open reading frames encoding potential homologues of Nudix hydrolases exist in Arabidopsis thaliana. Among them, AtNUDT1 (At1g68760) was initially characterized as a NADH pyrophosphatase (20). In addition, Klaus et al (21) recently reported that AtNUDT1 was the closest homologue of Lactococcus lactis YlgG and showed activities toward both dihydroneopterin triphosphate, a precursor of folate, and (deoxy)nucleoside triphosphates, including 8-oxo-dGTP.…”

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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

125

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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“…AtNUDT1 was previously reported to have activity toward NADH in the presence of 5 mM Mn 2ϩ (20). However, this activity was not detected in the presence of 5 mM Mg 2ϩ (Table I).…”

Section: Resultsmentioning

confidence: 70%

Section: Resultsmentioning

confidence: 99%

mentioning

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

125

170

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“…Exceptions include the Escherichia coli GDP-mannose mannosyl hydrolase, which is equally efficient with both Mg 2+ and Mn 2+ (Legler et al 2002) (Dobrzanska et al 2002). hDcp2 is the second example of a Nudix protein whose activity is greatly enhanced with Mn 2+ as the divalent cation.…”

Section: Discussionmentioning

confidence: 99%

Functional characterization of the mammalian mRNA decapping enzyme hDcp2

Piccirillo¹,

Khanna²,

Kiledjian³

2003

RNA

116

179

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Regulation of decapping is a critical determinant of mRNA stability. We recently identified hDcp2 as a human decapping enzyme with intrinsic decapping activity. This activity is specific to N 7 -methylated guanosine containing RNA. The hDcp2 enzyme does not function on the cap structure alone and is not sensitive to competition by cap analog, suggesting that hDcp2 requires the RNA for cap recognition. We now demonstrate that hDcp2 is an RNA-binding protein and its recognition and hydrolysis of the cap substrate is dependent on an initial interaction with the RNA moiety. A biochemical characterization of hDcp2 revealed that a 163 amino acid region containing two evolutionarily conserved regions, the Nudix fold hydrolase domain and the adjacent Box B region contained methyl-cap-specific hydrolysis activity. Maximum decapping activity for wild-type as well as truncation mutants of hDcp2 required Mn 2+ as a divalent cation. The demonstration that hDcp2 is an RNA-binding protein with an RNA-dependent decapping activity will now provide new approaches to identify specific mRNAs that are regulated by this decapping enzyme as well as provide novel avenues to control mRNA decapping and turnover by influencing the RNA-binding property of hDcp2.

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“…Saccharomyces cerevisiae Ysa1p and Arabidopsis thaliana AtNUDX2 and AtNUDX7 hydrolyze ADP-ribose and respond to oxidative stress (17,43). Nudix hydrolases that hydrolyze NAD ϩ and NADH [NAD(H)] exist throughout the biological kingdom and include A. thaliana AtNUDX1 (12) and yeast peroxisomal Npy1p (1). The physiological role of NAD(H) hydrolases is unknown, especially that in epigenetic gene regulation.…”

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confidence: 99%

Hydrolase Controls Cellular NAD, Sirtuin, and Secondary Metabolites

Shimizu

Masuo

Fujita

et al. 2012

Molecular and Cellular Biology

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Cellular levels of NAD؉ and NADH are thought to be controlled by de novo and salvage mechanisms, although evidence has not yet indicated that they are regulated by NAD ؉ degradation. Here we show that the conserved nudix hydrolase isozyme NdxA hydrolyzes and decreases cellular NAD ؉ and NADH in Aspergillus nidulans. The NdxA-deficient fungus accumulated more NAD ؉ during the stationary growth phase, indicating that NdxA maintains cellular NAD ؉ /NADH homeostasis. The deficient strain also generated less of the secondary metabolites sterigmatocystin and penicillin G and of their gene transcripts than did the wild type. These defects were associated with a reduction in acetylated histone H4 on the gene promoters of aflR and ipnA that are involved in synthesizing secondary metabolites. Thus, NdxA increases acetylation levels of histone H4. We discovered that the novel fungal sirtuin isozyme SirA uses NAD ؉ as a cosubstrate to deacetylate the lysine 16 residue of histone H4 on the gene promoter and represses gene expression. The impaired acetylation of histone and secondary metabolite synthesis in the NdxA-deficient strain were restored by eliminating functional SirA, indicating that SirA mediates NdxA-dependent regulation. These results indicated that NdxA controls total levels of NAD ؉ /NADH and negatively regulates sirtuin function and chromatin structure. N udix (nucleoside diphosphates linked to moiety X) hydrolases are ubiquitous in viruses, bacteria, and eukaryotes, and they hydrolyze NADH, NAD ϩ , ADP-ribose, and other nucleotide sugars, which allows their classification into subfamilies (6,22). One important function of nudix hydrolases is the hydrolytic degradation of oxidatively damaged nucleotides to prevent spontaneous mutations (39). Saccharomyces cerevisiae Ysa1p and Arabidopsis thaliana AtNUDX2 and AtNUDX7 hydrolyze ADP-ribose and respond to oxidative stress (17,43). Nudix hydrolases that hydrolyze NAD ϩ and NADH [NAD(H)] exist throughout the biological kingdom and include A. thaliana AtNUDX1 (12) and yeast peroxisomal Npy1p (1). The physiological role of NAD(H) hydrolases is unknown, especially that in epigenetic gene regulation.Gene expression is regulated by specific transcription regulators and by posttranslational modifications of nucleosomal histones. Acetylation is this type of modification that correlates with conformational changes in chromatin. Two groups of histone deacetylases (HDAC) deacetylate acetylated histones. One is classical HDAC, and the other is sirtuin, which deacetylates lysine residues of histones H3 and/or H4 using NAD ϩ as a cosubstrate (10,16,45). Yeast Sir2p is the prototype sirtuin, and it silences genes at mating type, ribosomal DNA (rDNA), and subtelomeric loci (14, 37). Its mammalian counterparts control aging, stress responses, and circadian rhythms (15, 25). Sirtuin activity is controlled by cellular NAD ϩ production (4, 19) that links cellular metabolic status and gene regulation, since NAD ϩ is a crucial coenzyme for biological redox reactions and energy conservat...

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Cloning and Characterization of the First Member of the Nudix Family from Arabidopsis thaliana

Cited by 27 publications

References 43 publications

Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana

Comprehensive Analysis of Cytosolic Nudix Hydrolases in Arabidopsis thaliana

Functional characterization of the mammalian mRNA decapping enzyme hDcp2

Hydrolase Controls Cellular NAD, Sirtuin, and Secondary Metabolites

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