Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1
Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1
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DOI：
10.1016/j.micinf.2007.07.008
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发表时间：
2007-10-01
影响因子：
5.8
通讯作者：
Kawaguchi, Yasushi
中科院分区：
文献类型：
--
作者：
Asa, Risa;Ohno, Takashi;Kawaguchi, Yasushi
单纯疱疹病毒I（HSV-1）UL 13是调节细胞培养物中的最佳病毒复制的病毒蛋白激酶。蛋白激酶底物的鉴定是阐明其功能机制的关键步骤。利用我们开发的系统分析UL 13的特异性蛋白激酶活性。我们已经表明，UL 13蛋白激酶直接磷酸化先前报道为假定底物的病毒蛋白ICP 22和UL 49。我们还确定了UL 41作为以前未报道的和新的底物的UL 13。这些数据将作为阐明UL 13影响病毒复制的机制的基础。(c)2007年，Elsevier Masson SAS。All rights reserved.
Herpes simplex virus 1 (HSV-1) UL 13 is a viral protein kinase that regulates optimal viral replication in cell cultures. Identification of substrates of protein kinases is a crucial step to elucidate the mechanism by which they function. Using our developed system to analyze the specific protein kinase activity of UL 13. we have shown that UL1 3 protein kinase directly phosphorylates the viral proteins ICP22 and UL49 previously reported to be putative substrates. We also identified UL41 as a previously unreported and novel substrate of UL13. These data will serve as a basis to clarify the mechanism by which UL13 influences viral replication. (c) 2007 Elsevier Masson SAS. All rights reserved.