title: Phosphorylation of nm23/nucleoside diphosphate kinase by casein kinase 2 in vitro.
abstract: We have investigated phosphorylation of human nucleoside diphosphate kinase (NDPK) and of homologous NDPK from different species by human casein kinase 2 (CK-2). The human NDPK isotypes A and B were phosphorylated by CK-2 in vitro both when the purified proteins and total lysate of HL-60 leukemia cells were used. The homologous NDPK's from Yeast and E. coli were also substrates for CK-2 in vitro, but not Drosophila NDPK. Phosphorylation of all NDPK types by the CK-2 holoenzyme was entirely polyamine-dependent. The CK-2 phosphorylation site in human NDPK A, that was about 2.5 times stronger phosphorylated than was the B isotype, was tentatively assigned to Ser-122. The location of the corresponding residue in the 3D-structure of the 80% homologous Drosophila NDPK suggests that its phosphorylation may directly influence substrate binding and/or catalysis.
authors.affiliation: Institut für Humangenetik, Universitätskliniken Geb. 68, Homburg, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Engel
authors.forename: O G
authors.initials: OG
authors.lastname: Issinger
authors.forename: I
authors.initials: I
authors.lastname: Lascu
authors.forename: T
authors.initials: T
authors.lastname: Seib
authors.forename: S
authors.initials: S
authors.lastname: Dooley
authors.forename: K D
authors.initials: KD
authors.lastname: Zang
authors.forename: C
authors.initials: C
authors.lastname: Welter
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D047388:Casein Kinases; D002460:Cell Line; D004330:Drosophila / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D015473:Leukemia, Promyelocytic, Acute; D008969:Molecular Sequence Data; D020559:Monomeric GTP-Binding Proteins; D054778:NM23 Nucleoside Diphosphate Kinases; D009701:Nucleoside-Diphosphate Kinase / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011107:Polylysine / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013096:Spermine / Q000494:pharmacology; D013379:Substrate Specificity; D014157:Transcription Factors / Q000302:isolation & purification / Q000378:metabolism*; D014407:Tumor Cells, Cultured
chemical_list: D054778:NM23 Nucleoside Diphosphate Kinases; D011994:Recombinant Proteins; D014157:Transcription Factors; D011107:Polylysine; D013096:Spermine; D011494:Protein Kinases; D047388:Casein Kinases; C517938:NME1 protein, human; D009701:Nucleoside-Diphosphate Kinase; D020559:Monomeric GTP-Binding Proteins