ACTIVATION OF M-PHASE-SPECIFIC HISTONE H1 KINASE BY MODIFICATION OF THE PHOSPHORYLATION OF ITS P34CDC2 AND CYCLIN COMPONENTS

被引：142

作者：

PONDAVEN, P ^{[1
]}

MEIJER, L ^{[1
]}

BEACH, D ^{[1
]}

机构：

[1] COLD SPRING HARBOR LAB,COLD SPRING HARBOR,NY 11724

来源：

GENES & DEVELOPMENT | 1990年 / 4卷 / 01期

关键词：

Cyclin; Histone HI kinase; P34[!sup]cdc2[!/sup;

D O I：

10.1101/gad.4.1.9

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

An M-phase-specific histone H1 kinase (H1K) has been described in a wide variety of eukaryotic cell types undergoing the G2/M transition in the cell division cycle. We have used p13suc1-Sepharose affinity chromatography to purify H1K to near homogeneity from matured starfish oocytes. A yield of 67% was obtained. Active H1K behaves as a 90- to 100-kD protein and appears to be constituted of equimolar amounts of cyclin and p34cdc2. The p34cdc2 subunit becomes tyrosine-dephosphorylated as the H1K is activated during entry of the oocytes into M phase, whereas the cyclin subunit is reciprocally phosphorylated. Acid phosphatase treatment of inactive p34cdc2/cyclin complex induces p34cdc2 dephosphorylation and three- to eightfold stimulation of the enzyme activity. These results suggest that active M-phase-specific H1K is constituted of both dephosphorylated p34cdc2 and phosphorylated cyclin.

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页码：9 / 17

页数：9

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