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NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3 (1999)

Mehus, James G. ; Deloukas, Panagiotis ; Lambeth, D. O.

Springer

Human genetics 〈Berlin〉 104 (1999), S. 454-459

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ISSN: 1432-1203

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Abstract The NME (nm23/nucleoside diphosphate kinase) gene family in human is involved in the phosphorylation of nucleoside diphosphates and a variety of regulatory phenomena associated with development, oncogenic transformation, and metastasis. Here we report the cDNA sequence for a sixth member of this family, NME6. The cDNA sequence predicts a 186-residue protein that includes the characteristic active site motif of a nucleoside diphosphate (NDP) kinase, as well as the other residues previously identified as crucial for nucleotide binding and catalysis. The NME6 protein sequence is only 34–41% identical to the five previously reported human NME proteins, and is similarly related to prokaryotic and primitive eukaryotic NDP kinases. Compared to typical proteins of this family such as NME1 and NME2, NME6 has three additional residues located in the Kpn loop, and a 22-residue extension at the COOH-terminal. Using radiation hybrid mapping, the NME6 gene was localized to chromosome 3p21.3. The 1.3-kb transcript of NME6 is expressed at a moderately low level in many human tissues, and is most abundant in kidney, prostate, ovary, intestine, and spleen. Homologous cDNAs were also cloned and sequenced for rat and mouse. The sequence of the first 171 residues of the mouse homologue (Nm23-M6) is 94% identical to the deduced human NME6 protein.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s004390050987

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The Human Nm23/Nucleoside Diphosphate Kinases (2000)

Lacombe, Marie-Lise Laurence ; Munier, Annie ; Mehus, James G. ; [et al.]

Springer

Journal of bioenergetics and biomembranes 32 (2000), S. 247-258

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ISSN: 1573-6881

Keywords: Nm23 ; NDP kinase ; mitochondria ; testis ; dynein ; metastasis

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Physics

Notes: Abstract Biochemical experiments over the past 40 years have shown that nucleoside diphosphate(NDP) kinase activity, which catalyzes phosphoryl transfer from a nucleoside triphosphate toa nucleoside diphosphate, is ubiquitously found in organisms from bacteria to human. Overthe past 10 years, eight human genes of the nm23/NDP kinase family have been discoveredthat can be separated into two groups based on analysis of their sequences. In addition tocatalysis, which may not be exhibited by all isoforms, evidence for regulatory roles has comerecently from the discovery of the genes nm23 and awd, which encode NDP kinases and areinvolved in tumor metastasis and Drosophila development, respectively. Current work showsthat the human NDP kinase genes are differentially expressed in tissues and that their productsare targeted to different subcellular locations. This suggests that Nm23/NDP kinases possessdifferent, but specific, functions within the cell, depending on their localization. The roles ofNDP kinases in metabolic pathways and nucleic acid synthesis are discussed.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1005584929050

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