CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15.
CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15.
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CAK 是 p34cdc2 激活激酶，含有与 p40MO15 相同或密切相关的蛋白质。
DOI：
10.1002/j.1460-2075.1993.tb05982.x
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Shuttleworth,J
中科院分区：
文献类型：
--
作者：
Solomon,MJ;Harper,JW;Shuttleworth,J
有丝分裂诱导剂p34cdc2需要与细胞周期蛋白结合，并在Thr161上磷酸化才能发挥其作为蛋白激酶的活性。CAK， p34cdc2活化激酶，先前被确定为这种活化磷酸化所必需的酶。我们在这里证实了CAK是一种蛋白激酶，并描述了其从爪蟾卵提取物中纯化的13000倍以上。我们进一步发现，CAK含有一种与先前鉴定的爪蟾MO15基因相同或密切相关的蛋白质：p40MO15与CAK结合，p40MO15的抗血清特异性地消耗CAK的活性。CAK似乎是爪蟾卵提取物中唯一可以激活p34cdc2或与其密切相关的蛋白激酶p33cdk2与周期蛋白A或周期蛋白b复合物的蛋白。p40MO15与p34cdc2序列相似，且CAK的大小约为200 kDa，这表明p40MO15本身可能受亚基结合和蛋白磷酸化的调节。
The mitotic inducer p34cdc2 requires association with a cyclin and phosphorylation on Thr161 for its activity as a protein kinase. CAK, the p34cdc2 activating kinase, was previously identified as an enzyme necessary for this activating phosphorylation. We confirm here that CAK is a protein kinase and describe its purification over 13,000‐fold from Xenopus egg extracts. We further show that CAK contains a protein identical or closely related to the previously identified Xenopus MO15 gene: p40MO15 copurifies with CAK, and an antiserum to p40MO15 specifically depletes cAK activity. CAK appears to be the only protein in Xenopus egg extracts that can activate complexes of either p34cdc2 or the closely related protein kinase, p33cdk2, with either cyclin A or cyclin B. The sequence similarity between p40MO15 and p34cdc2, and the approximately 200 kDa size of CAK, suggest that p40MO15 may itself be regulated by subunit association and by protein phosphorylations.