DNA-ACTIVATED PROTEIN-KINASE IN BURKITT,RAJI LYMPHOMA-CELLS - PHOSPHORYLATION OF C-MYC ONCOPROTEIN

被引：48

作者：

IIJIMA, S ^{[1
]}

TERAOKA, H ^{[1
]}

DATE, T ^{[1
]}

TSUKADA, K ^{[1
]}

机构：

[1] KANAZAWA MED UNIV, INST MED RES, UCHINADA, ISHIKAWA, JAPAN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 206卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb16964.x

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：

Autophosphorylation of a DNA-activated protein kinase (DNA-PK) in Raji Burkitt's lymphoma cells generated a band that corresponded to a phosphoprotein of about 300 kDa on SDS/PAGE. This band corresponds to a 300-350-kDa DNA-PK found previously in HeLa cells. In addition to the 300-kDa phosphoprotein, the band of a highly phosphorylated 58-kDa protein was detected by SDS/PAGE of partially purified DNA-PK preparations after the phosphorylation reaction in the presence of double-stranded DNA. This phosphoprotein was specifically immunoprecipitated by mAb against c-Myc. More highly purified preparations of DNA-PK, containing neither a 58-kDa phosphoprotein nor detectable activities of other kinases, phosphorylated recombinant c-Myc proteins in the presence of DNA. The c-Myc phosphorylation by DNA-PK was markedly stimulated by relaxed, double-stranded DNA, but neither by single-stranded DNA nor by RNA. Phosphopeptide mapping and phosphoamino acid analysis indicated that DNA-PK phosphorylates c-Myc in vitro at several serine residues.

引用

页码：595 / 603

页数：9

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