Peptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylated.
Peptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylated.
复制标题
含有源自病毒起始蛋白的细胞周期蛋白/Cdk 核定位信号基序的肽在未磷酸化时与 DNA 结合。
DOI：
10.1128/jvi.76.23.11785-11792.2002
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发表时间：
2002
影响因子：
5.4
通讯作者：
Bullock,PeterA
中科院分区：
文献类型：
--
作者：
Kim,RonaldJ;Moine,Stephanie;Reese,DanielleK;Bullock,PeterA
T 抗原残基 Thr124 处的单个磷酸化事件调节猿病毒 40 DNA 复制的启动。为了探索这一调节过程，合成了一系列以 Thr124 为中心的肽。这些肽含有核定位信号 (NLS) 和细胞周期蛋白/Cdk 激酶的识别位点。当未磷酸化时，“CDK/NLS”肽会抑制 T 抗原组装并将非序列特异性结合到 DNA。然而，这些活性在 Thr124 磷酸化后大大降低。使用源自牛乳头瘤病毒 E1 的 CDK/NLS 区域的肽也获得了类似的结果。相关研究表明，NLS 中的残基与 DNA 结合，而 CDK 基序中的残基则调节结合。这些发现从 T 抗原双六聚体组装的控制和病毒复制的启动方面进行了讨论。
A single phosphorylation event at T-antigen residue Thr124 regulates initiation of simian virus 40 DNA replication. To explore this regulatory process, a series of peptides were synthesized, centered on Thr124. These peptides contain a nuclear localization signal (NLS) and a recognition site for cyclin/Cdk kinases. When unphosphorylated, the “CDK/NLS” peptides inhibit T-antigen assembly and bind non-sequence specifically to DNA. However, these activities are greatly reduced upon phosphorylation of Thr124. Similar results were obtained by using peptides derived from the CDK/NLS region of bovine papillomavirus E1. Related studies indicate that residues in the NLS bind to DNA, whereas those in the CDK motif regulate binding. These findings are discussed in terms of the control of T-antigen double hexamer assembly and initiation of viral replication.