Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1
Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1
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DOI：
10.1128/jvi.79.14.9325-9331.2005
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发表时间：
2005-07-01
影响因子：
5.4
通讯作者：
Kawaguchi, Y
中科院分区：
文献类型：
--
作者：
Kato, A;Yamamoto, M;Kawaguchi, Y
我们已经开发了一个系统来分析特异性蛋白激酶活性的单纯疱疹病毒1型Us3在体外，并表明，Us3直接磷酸化病毒蛋白UL34，ICP22，和Us9和细胞蛋白质坏，以前报道的推定底物。使用该系统，我们确定了UL34的磷酸化位点，并将UL31鉴定为以前未报道的Us3的新底物。该系统将有助于进一步鉴定Us3底物及其磷酸化位点，阐明Us3在病毒复制中的作用，并鉴定其他Us3功能。
We have developed a system to analyze the specific protein kinase activity of herpes simplex virus 1 Us3 in vitro and shown that Us3 directly phosphorylates viral proteins UL34, ICP22, and Us9 and the cellular protein Bad, previously reported to be putative substrates. Using this system, we determined the phosphorylation sites of UL34 and identified UL31 as a previously unreported, novel substrate of Us3. This system will be useful for further identification of Us3 substrates and their phosphorylation sites, clarification of the role of Us3 in viral replication, and identification of additional Us3 function(s).