Nudix hydrolases are a family of proteins defined by conserved amino-acid sequence GX(5)-EX(7)REUXEEXGU, where U is hydrophobic residue. These enzymes widely distributed among all classes organisms and catalyze, with varying degrees substrate specificity, the hydrolysis variety nucleoside diphosphate derivatives: di- triphosphates their oxidized forms, dinucleoside polyphosphates, nucleotide sugars, NADH, coenzyme A mRNA cap. postulated to control cellular concentration these compounds. The...

The sequence motif commonly called a Nudix box, represented by (GX(5)EX(7)REVXEEXGU) is the marker of widely distributed family enzymes that catalyze hydrolysis variety nucleoside diphosphate derivatives. Here we describe cloning and characterization an Arabidopsis thaliana cDNA encoding hydrolase degrades NADH. deduced amino acid AtNUDT1 contains 147 acids. recombinant was expressed in Escherichia coli purified. In presence Mn(2+) optimal pH 7. 0, catalyzed NADH with K(m) value 0. 36 mm. A...

A cDNA corresponding to the At3g26690 gene, which encodes a Nudix protein (AtNUDT13) with predicted mitochondrial localization, was isolated from an Arabidopsis thaliana library. The 202 amino acid AtNUDT13 polypeptide overexpressed in Escherichia coli and purified homogeneity. preferred substrate for this hydrolase diadenosine hexaphosphate (Ap(6)A), K(m) k(cat)/K(m) values of 0.61 mm 16.0 x 10(3) m(-)1.s(-1), respectively. Optimal activity at alkaline pH (8.5) Mg(2+) (5 mm) as cofactor. MS...

Arabidopsis thaliana AtNUDT7 Nudix pyrophosphatase hydrolyzes NADH and ADP-ribose in vitro is an important factor the cellular response to diverse biotic abiotic stresses. Several studies have shown that loss-of-function Atnudt7 mutant plants display many profound phenotypes. However molecular mechanism of function remains elusive. To gain a better understanding this hydrolase role, proteins interacting with were identified. Using as bait binding assay derived from cultured cell extracts we...

Abstract Nudix proteins catalyze the hydrolysis of pyrophosphate bonds in a variety substrates and are ubiquitous all domains life. The genome an important opportunistic human pathogen, Pseudomonas aeruginosa , encodes multiple proteins. To determine role nine hydrolases P. PAO1161 strain its fitness, virulence or antibiotic resistance mutants devoid individual enzymes were constructed analyzed for growth rate, motility, biofilm formation, pyocyanin production, susceptibility to oxidative...

Summary The PA0336 protein from Pseudomonas aeruginosa belongs to the family of widely distributed Nudix pyrophosphohydrolases, which catalyze hydrolysis pyrophosphate bonds in a variety nucleoside diphosphate derivatives. amino acid sequence is highly similar that RppH RNA pyrophosphohydrolase Escherichia coli , removes 5′‐end triphosphorylated transcripts. Trans‐complementation experiments showed P. enzyme can functionally substitute for E. cells indicating that, RppH, hydrolase mediates...

Summary Nudix pyrophosphatases, ubiquitous in all organisms, have not been well studied. Recent implications that some of them may be involved response to stress and pathogenesis indicate they play important biological functions. We investigated NudC proteins from the plant pathogen P seudomonas syringae pv. tomato str. DC 3000 human aeruginosa PAO 1161. found these homologous enzymes are homodimeric vitro preferentially hydrolyse NADH . The mutant strain deficient accumulated displayed...

Arabidopsis thaliana AtNUDT7, a homodimeric Nudix hydrolase active on ADP-ribose and NADH, exerts negative control the major signaling complex involved in plant defense activation programmed cell death. The structural functional consequences of altering several amino-acid residues AtNUDT7 protein have been examined by site-directed mutagenesis, far-UV circular dichroism (CD), attenuated total reflection-Fourier transform infrared (ATR-FTIR) photon correlation (PCS) spectroscopy, biochemical...

For nearly half of the proteome an important pathogen, Pseudomonas aeruginosa, function has not yet been recognised. Here, we characterise one such mysterious protein PA2504, originally isolated by us as a sole partner RppH RNA hydrolase involved in transcription regulation multiple genes. This study aims at elucidating details PA2504 and discussing its implications for bacterial biology. We show that forms homodimers is evenly distributed cytoplasm cells. Molecular modelling identified...

A cloned genomic DNA fragment (pTa241) formerly derived from a fraction obtained isolated nuclei of embryos Polish cultivar wheat (Triticum aestivum cv. Begra) comprises tandem repeat the telomeric array CCCTAAA, and hybridizes in situ exclusively to telomeres all chromosome arms somatic complement wheat. second (pTa637) same is 637 bp long, flanked by 28 unit, entire lengths chromosomes complement. The pattern hybridization was observed when flanking sequences were removed. third (pTa1439),...

A reverse transcriptase-like activity was isolated from germinating wheat (Triticum aestivum) embryos. The found to be associated with a microsomal fraction (70,000 g pellet) of the embryo homogenate. microsome-associated enzyme prefers homologous polyadenylated RNA any other polynucleotides as template and requires all four deoxyribonucleoside triphosphates for maximal activity. reaction product appears in incubation mixture form an RNA-DNA hybrid, which can converted into single-stranded...

A cloned genomic DNA fragment (pTa241) formerly derived from a fraction obtained isolated nuclei of embryos Polish cultivar wheat (Triticum aestivum cv. Begra) comprises tandem repeat the telomeric array CCCTAAA, and hybridizes in situ exclusively to telomeres all chromosome arms somatic complement wheat. second (pTa637) same is 637 bp long, flanked by 28 unit, entire lengths chromosomes complement. The pattern hybridization was observed when flanking sequences were removed. third (pTa1439),...