Phosphorylation of bovine papillomavirus E1 by the protein kinase CK2 near the nuclear localization signal does not influence subcellular distribution of the protein in dividing cells.
Phosphorylation of bovine papillomavirus E1 by the protein kinase CK2 near the nuclear localization signal does not influence subcellular distribution of the protein in dividing cells.
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DOI：
10.1007/s00705-015-2641-6
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发表时间：
2016-01
影响因子：
2.7
通讯作者：
Shideler T
中科院分区：
文献类型：
--
作者：
Lentz MR;Shideler T
牛乳头瘤病毒 E1 解旋酶对于病毒复制至关重要。在分裂细胞中，DNA 复制维持病毒基因组拷贝数，但不会增加。复制受到低 E1 表达和 E1 核质穿梭机制的限制。穿梭部分由细胞激酶对 E1 的磷酸化进行控制。在这里，我们研究了 E1 核定位信号内激酶 CK2 磷酸化的保守位点。当这些 CK2 位点突变为丙氨酸或天冬氨酸时，没有观察到复制表型的变化，并且对 E1 的亚细胞分布没有影响，E1 仍然主要在细胞核中分布。这表明 CK2 在这些位点对 E1 的磷酸化并不是调节分裂细胞中病毒 DNA 复制的因素。
The bovine papillomavirus E1 helicase is essential for viral replication. In dividing cells, DNA replication maintains, but does not increase, the viral genome copy number. Replication is limited by low E1 expression and an E1 nucleocytoplasmic shuttling mechanism. Shuttling is controlled in part by phosphorylation of E1 by cellular kinases. Here we investigate conserved sites for phosphorylation by kinase CK2 within the E1 nuclear localization signal. When these CK2 sites are mutated to either alanine or aspartic acid, no change in replication phenotype is observed, and there is no effect on the subcellular distribution of E1, which remains primarily nuclear. This demonstrates that phosphorylation of E1 by CK2 at these sites is not a factor in regulating viral DNA replication in dividing cells.