Crystal structure of the Awd nucleotide diphosphate kinase from Drosophila

Chiadmi, M.; Moréra, Solange; Lascu, Ioan; Dumas, Christian; Bras, Gisèle Le; Véron, Michel; Janin, Joël

doi:10.1016/0969-2126(93)90016-a

Cited by 98 publications

(87 citation statements)

References 28 publications

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“…In human cells, four members of the NDP kinase family encoded by the genes nm23-H 1 (8), nm23-H 2 (9), DR-nm23 (10), and nm23-H 4 (11) have been identified so far. A fifth isoform, nm23-H 5 was isolated very recently but it does not exhibit NDP kinase activity when overexpressed in bacteria (12).…”

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confidence: 99%

“…They catalyze the transfer of a phosphate from a nucleoside triphosphate to a nucleoside diphosphate via the formation of an enzymatic intermediate phosphorylated on a catalytic histidine residue (1). The crystal structures of NDP 1 kinases from several organisms including prokaryotes (2) and eukaryotes (3)(4)(5) have been determined. They all share a common subunit fold, built around a ␤␣␤␤␣␤ motif, also present in the "palm domain" of DNA polymerases (5).…”

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confidence: 99%

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Single Strand DNA Specificity Analysis of Human Nucleoside Diphosphate Kinase B

Agou

Raveh

Mesnildrey

et al. 1999

Journal of Biological Chemistry

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Nucleoside diphosphate kinases (NDP kinases) form a family of oligomeric enzymes present in all organisms. Eukaryotic NDP kinases are hexamers composed of identical subunits (Ϸ17 kDa). A distinctive property of human NDPK-B encoded by the gene nm23-H 2 is its ability to stimulate the gene transcription. This property is independent of its catalytic activity and is possibly related to the role of this protein in cellular events including differentiation and tumor metastasis. In this paper, we report the first characterization of human NDPK-B⅐DNA complex formation using a filter-binding assay and fluorescence spectroscopy. We analyzed the binding of several oligonucleotides mimicking the promoter region of the c-myc oncogene including variants in sequence, structure, and length of both strands. We show that NDPK-B binds to single-stranded oligonucleotides in a nonsequence specific manner, but that it exhibits a poor binding activity to double-stranded oligonucleotides. This indicates that the specificity of recognition to DNA is a function of the structural conformation of DNA rather than of its specific sequence. Moreover, competition experiments performed with all nucleotides provide evidence for the contribution of the six active sites in the DNA⅐protein complex formation. We propose a mechanism through which human NDPK-B could stimulate transcription of c-myc or possibly other genes involved in cellular differentiation.

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confidence: 99%

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Single Strand DNA Specificity Analysis of Human Nucleoside Diphosphate Kinase B

Agou

Raveh

Mesnildrey

et al. 1999

Journal of Biological Chemistry

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“…The currently known high-resolution crystal structures of NDPK are: tetrameric: Myxococcus xanthus [ 18]; hexameric: Dictyostelium discoideum [19], Drosophila melanogaster [20] and Homo sapiens nm23-H2, NDPK-HB [21]. However, Hamby et al [22] report NDPK-HB to be tetrameric in solution and preliminary gel filtration studies in our laboratory also suggested a smaller complex than a hexamer for NDPK-HB.…”

Section: Introductionmentioning

confidence: 78%

Quaternary structure of human nucleoside diphosphate kinase isoforms HA and HB in solution

Schaertl

1996

FEBS Letters

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“…The crystal structure of Drosophila melanogaster awd and of Dictyostelium discoideum NDPK has been resolved (Chiadmi et al, 1993;Dumas et al, 1992). The enzyme is a symmetrical hexamer of identical subunits.…”

Section: Introductionmentioning

confidence: 99%

Evidence for interaction between human PRUNE and nm23-H1 NDPKinase

et al. 1999

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We have isolated a human and murine homologue of the Drosophila prune gene through dbEST searches. The gene is ubiquitously expressed in human adult tissues, while in mouse developing embryos a high level of expression is con®ned to the nervous system particularly in the dorsal root ganglia, cranial nerves, and neural retina. The gene is composed of eight exons and is located in the 1q21.3 chromosomal region. A pseudogene has been sequenced and mapped to chromosomal region 13q12. PRUNE protein retains the four characteristic domains of DHH phosphoesterases. The synergism between prune and awd K-pn in Drosophila has led various authors to propose an interaction between these genes. However, such an interaction has never been supported by biochemical data. By using interaction-mating and in vitro co-immunoprecipitation experiments, we show for the ®rst time the ability of human PRUNE to interact with the human homologue of awd protein (nm23-H1). In contrast, PRUNE is impaired in its interaction with nm-23-H1-S120G mutant, a gain-of-function mutation associated with advanced neuroblastoma stages. Consistently, PRUNE and nm23-H1 proteins partially colocalize in the cytoplasm. The data presented are consistent with the view that PRUNE acts as a negative regulator of the nm23-H1 protein. We discuss how PRUNE regulates nm23-H1 protein and postulate possible implications of PRUNE in neuroblastoma progression.

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Crystal structure of the Awd nucleotide diphosphate kinase from Drosophila

Cited by 98 publications

References 28 publications

Single Strand DNA Specificity Analysis of Human Nucleoside Diphosphate Kinase B

Single Strand DNA Specificity Analysis of Human Nucleoside Diphosphate Kinase B

Quaternary structure of human nucleoside diphosphate kinase isoforms HA and HB in solution

Evidence for interaction between human PRUNE and nm23-H1 NDPKinase

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