PHOSPHORYLATION OF NM23/NUCLEOSIDE DIPHOSPHATE KINASE BY CASEIN KINASE-2 IN-VITRO

被引:18
作者
ENGEL, M [1 ]
ISSINGER, OG [1 ]
LASCU, I [1 ]
SEIB, T [1 ]
DOOLEY, S [1 ]
ZANG, KD [1 ]
WELTER, C [1 ]
机构
[1] UNIV BORDEAUX 2,CNRS,IBC,F-33077 BORDEAUX,FRANCE
关键词
D O I
10.1006/bbrc.1994.1334
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1994 Academic Press, Inc.
引用
收藏
页码:1041 / 1048
页数:8
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