Phosphorylation by protein kinase CK2 changes the DNA binding properties of the human chromatin protein DEK
Phosphorylation by protein kinase CK2 changes the DNA binding properties of the human chromatin protein DEK
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DOI：
10.1128/mcb.24.13.6011-6020.2004
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发表时间：
2004-07-01
影响因子：
5.3
通讯作者：
Gruss, C
中科院分区：
文献类型：
--
作者：
Kappes, F;Damoc, C;Gruss, C
我们研究了人染色质蛋白DEK的翻译后修饰，发现在体外和体内DEK都被蛋白激酶CK 2磷酸化。磷酸化位点被映射的四极杆离子阱质谱，并发现在C-末端区域的DEK蛋白聚集。磷酸化在细胞周期中波动，在G1期有一个中等的峰。滤纸结合试验以及Southwestern分析表明，磷酸化减弱了DEK与DNA的结合。然而，在体内，磷酸化的DEK保留在染色质上。我们目前的证据表明，磷酸化的DEK是拴在染色质在整个细胞周期的非或磷酸化不足的形式的DEK。
We have examined the posttranslational modification of the human chromatin protein DEK and found that DEK is phosphorylated by the protein kinase CK2 in vitro and in vivo. Phosphorylation sites were mapped by quadrupole ion trap mass spectrometry and found to be clustered in the C-terminal region of the DEK protein. Phosphorylation fluctuates during the cell cycle with a moderate peak during G, phase. Filter binding assays, as well as Southwestern analysis, demonstrate that phosphorylation weakens the binding of DEK to DNA. In vivo, however, phosphorylated DEK remains on chromatin. We present evidence that phosphorylated DEK is tethered to chromatin throughout the cell cycle by the un- or underphosphorylated form of DEK.