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AN INHIBITOR OF P34(CDC28) PROTEIN-KINASE ACTIVITY FROM SACCHAROMYCES-CEREVISIAE
被引:176
作者:
MENDENHALL, MD
[1
]
机构:
[1] UNIV KENTUCKY,DEPT BIOCHEM,LEXINGTON,KY 40536
来源:
关键词:
D O I:
10.1126/science.8421781
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
The p34CDC28 protein from Saccharomyces cerevisiae is a homolog of the p34cdc2 protein kinase, a fundamental regulator of cell division in all eukaryotic cells. Once activated it initiates the visible events of mitosis (chromosome condensation, nuclear envelope breakdown, and spindle formation). The p34CDC28 protein also has a critical role in the initiation of DNA synthesis. The protein kinase activity is regulated by cycles of phosphorylation and dephosphorylation and by periodic association with cyclins. An endogenous 40-kilodalton protein (p40) originally identified as a substrate of the p34CDC28 protein kinase was purified. The p40 protein bound tightly to p34CDC28 and inhibited the activity of the kinase. The p40 protein may provide another mechanism to regulate p34CDC28 protein kinase activity.
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页码:216 / 219
页数:4
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