Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the <i>DRnm23</i> gene

Erent, Muriel; Gonin, Philippe; Cherfils, Jacqueline; Tissier, Pierre; Raschellà, Giuseppe; Giartosio, Anna; Agou, Fabrice; Sarger, Claude; Lacombe, Marie−Lise; Konrad, Manfred; Lascu, Ioan

doi:10.1046/j.1432-1327.2001.2076.doc.x

Cited by 21 publications

(18 citation statements)

References 50 publications

(54 reference statements)

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“…The tag at the C-terminus would not interfere with the organellar targeting, though it may possibly disturb the proper oligomerization of the enzyme, known to be required for the expression of its enzymatic activity in either tetra-or hexameric state. DtNDK1 displays at the C-terminus the tyrosine-glutamate (YE) motif assumed to be necessary in the hexamer assembly (Erent et al 2001). This motif is not present in the organellar NDP kinase isoforms reported to date, except for the Dictyostelium mitochondrial one (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The conserved residues within all sequences are shown in white on a black background. Similar residues are indicated in black on a gray background and the asterisks mark the residues important for the hexameric structure (Erent et al 2001). The residues involved in catalysis (Cherfils et al 1994, Dumas et al 1992, Tepper et al 1994 are marked with an "a".…”

Section: Expression and Purification Of Dtndk1 Proteinsmentioning

confidence: 99%

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Identification of a Mitochondrial Nucleoside Diphosphate Kinase from the Green Alga Dunaliella tertiolecta

Anderca

Furuichi

Pinontoan

et al. 2002

Plant and Cell Physiology

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;We isolated a full-length cDNA encoding a nucleoside diphosphate (NDP) kinase from a Dunaliella tertiolecta cDNA library by homology cloning and rapid amplification of cDNA ends-PCR. The cDNA sequence, consisting of 840 bp, contained an open reading frame coding for a 221-amino acid protein. The predicted 24-kDa protein was named DtNDK1. It possesses all the residues involved in nucleotide binding and catalysis and, in its long N-terminus, contains putative mitochondrial targeting peptides. The full-length pre-protein expressed in Escherichia coli as a recombinant N-terminally His-tagged protein was retained in inclusion bodies, totally devoid of NDP kinase activity. Upon expression in yeast cells, the full-length protein His-tagged at the C-terminus was found processed in a soluble form that was lacking the first 67 amino acids from the N-terminus. The mature protein, which was purified by affinity chromatography to near homogeneity, showed NDP kinase activity. Confocal microscopy on yeast cells expressing the recombinant protein revealed the specific mitochondrial localization of DtNDK1 labeled at the C-terminus with green fluorescent protein.

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Section: Discussionmentioning

confidence: 99%

Section: Expression and Purification Of Dtndk1 Proteinsmentioning

confidence: 99%

Identification of a Mitochondrial Nucleoside Diphosphate Kinase from the Green Alga Dunaliella tertiolecta

Anderca

Furuichi

Pinontoan

et al. 2002

Plant and Cell Physiology

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“…Since the NDK family is highly conserved both at the primary protein sequence level (Fig. 3) and at the protein structure level (4,12,15,17,21,33,43,48,68,69), we were able to predict the protein structure of SwoHp using homology modeling. Like other NDKs, SwoHp is predicted to have a core of four internal ␤-strands surrounded by 6 ␣-helices (Fig.…”

Section: Vol 2 2003 Ndk Is Essential In a Nidulans 1173mentioning

confidence: 99%

SwoHp, a Nucleoside Diphosphate Kinase, Is Essential inAspergillus nidulans

Lin¹,

Momany

Momany³

2003

Eukaryot Cell

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The temperature-sensitive swoH1 mutant of Aspergillus nidulans was previously identified in a screen for mutants with defects in polar growth. In the present work, we found that the swoH1 mutant swelled, lysed, and did not produce conidia during extended incubation at the restrictive temperature. When shifted from the permissive to the restrictive temperature, swoH1 showed the temperature-sensitive swelling phenotype only after 8 h at the higher temperature. The swoH gene was mapped to chromosome II and cloned by complementation of the temperature-sensitive phenotype. The sequence showed that swoH encodes a homologue of nucleoside diphosphate kinases (NDKs) from other organisms. Deletion experiments showed that the swoH gene is essential. A hemagglutinin-SwoHp fusion complemented the mutant phenotype, and the purified fusion protein possessed phosphate transferase activity in thin-layer chromatography assays. Sequencing of the mutant allele showed a predicted V83F change. Structural modeling suggested that the swoH1 mutation would lead to perturbation of the NDK active site. Crude cell extracts from the swoH1 mutant grown at the permissive temperature had ϳ20% of the NDK activity seen in the wild type and did not show any decrease in activity when assayed at higher temperatures. Though the data are not conclusive, the lack of temperature-sensitive NDK activity in the swoH1 mutant raises the intriguing possibility that the SwoH NDK is required for growth at elevated temperatures rather than for polarity maintenance.Spores of the filamentous fungus Aspergillus nidulans break dormancy and expand isotropically before sending out a germ tube and switching to polar-tip growth. Further growth occurs exclusively at the hyphal tip (45). The temperature-sensitive swoH1 mutant of A. nidulans was originally isolated in a screen for polarity maintenance defects (46) based on the fact that the mutant hyphae swell shortly after germ tube emergence at the restrictive temperature. The sequence of the swoH gene reveals that it encodes a homologue of yeast YNK1, a nucleoside diphosphate kinase (NDK). NDKs catalyze the transfer of the ␥-phosphate from a nucleoside triphosphate to a nucleoside diphosphate and are important in nucleotide metabolism (2, 28).NDK null mutants of Escherichia coli and Pseudomonas aeruginosa are viable (27,87). NDK null mutants of Saccharomyces cerevisiae and Schizosaccharomyces pombe are normal in vegetative growth, sporulation, mating, and morphology, though they have much lower NDK activity than the wild types (10 and 20%, respectively) (19,27). Enzymes other than NDK are assumed to furnish these low levels of NDK activity (19,32,38,55,77,84). The only reported NDK mutation in a filamentous fungus, a P72H change in Neurospora crassa, causes reduced NDK activity and deficient light response for perithecial polarity (57, 58). In plants, NDK interacts with phytochromes, photoreceptors that relay environmental light signals to nuclear genes (13,26,73). Higher organisms contain multiple isoforms of NDK, some...

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“…It is ubiquitously expressed (21) and active as a hexamer, like the cytosolic NDPK-A, -B, and -C isoforms (22,25). Information on its precise localization and function is scarce, except its peripheral association with mitochondrial membranes (22), a putative association with STK (26), and an overexpression noted in colorectal carcinomas (27).…”

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confidence: 99%

The Nucleoside Diphosphate Kinase D (NM23-H4) Binds the Inner Mitochondrial Membrane with High Affinity to Cardiolipin and Couples Nucleotide Transfer with Respiration

Tokarska‐Schlattner

Boissan

Munier

et al. 2008

Journal of Biological Chemistry

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109

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Nucleoside diphosphate kinases (NDPK), 3 encoded by NME genes (also called NM23), catalyze the exchange of ␥-phosphate between di-and triphosphonucleosides and participate in the regulation of intracellular nucleotide homeostasis. They mainly utilize ATP formed by oxidative phosphorylation to synthesize the other triphosphonucleosides, in particular GTP (1). Given the poor substrate selectivity of NDPKs, it is assumed that specificity could arise from the presence of different isoforms at different subcellular localizations. Associated in networks with other nucleotide-metabolizing enzymes such as adenylate kinases, creatine kinases, and glycolytic enzymes, NDPKs participate in high energy phosphoryl transfer and signal communication in the cell (2). Up to now nine genes encoding NDPK or NDPK-like proteins have been identified (3, 4), but little is known about their respective role within the cell. The most studied, NDPK-A and -B, encoded by NME1 and NME2 genes, respectively, play a key role in tumor progression and metastasis dissemination (5, 6).NDPK activity has been found associated with different cellular compartments, such as cytosol, nucleus, plasma membrane, and mitochondria. Precise localization in the latter organelles has been a matter of debate. Depending on species and tissue examined, NDPK activity was reported in both the matrix and the intermembrane/cristae space (7), including the so-called contact sites between inner and outer membrane (8 -10). In mammalian liver (rat and rabbit), the NDPK activity was mainly associated with an extra-matrix compartment, probably the intermembrane/cristae space, whereas in heart activity was more abundant in the matrix (11). For mitochondrial NDPK in matrix, many functions have been proposed ranging from nucleotide supply for mitochondrial nucleic acid and protein synthesis to functional interaction with the Krebs * This work was supported by the Germaine de Stael Program for FrancoSwiss collaboration (to U. S. and M.-L. L.), the Agence Nationale de la Recherche (Chaire d'Excellence (to U. S.)), the Marie Curie Intraeuropean Fellowship of the European Community (to M. T.-S.), INSERM, and grants from the Groupement des Entreprises Françaises contre le Cancer and from the Association pour la Recherche contre le Cancer (to M.-L. L.). 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.

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Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene

Cited by 21 publications

References 50 publications

Identification of a Mitochondrial Nucleoside Diphosphate Kinase from the Green Alga Dunaliella tertiolecta

Identification of a Mitochondrial Nucleoside Diphosphate Kinase from the Green Alga Dunaliella tertiolecta

SwoHp, a Nucleoside Diphosphate Kinase, Is Essential inAspergillus nidulans

The Nucleoside Diphosphate Kinase D (NM23-H4) Binds the Inner Mitochondrial Membrane with High Affinity to Cardiolipin and Couples Nucleotide Transfer with Respiration

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