Characterization of nuclear localization signals of the prototype foamy virus integrase
Characterization of nuclear localization signals of the prototype foamy virus integrase
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DOI：
10.1099/vir.0.83689-0
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发表时间：
2008-07-01
影响因子：
3.8
通讯作者：
Shin, Cha-Gyun
中科院分区：
文献类型：
--
作者：
An, Dog Gn;Hyun, Usok;Shin, Cha-Gyun
为了分析原型泡沫病毒（PFV）的潜在亲核活性，我们将 PFV 整合酶（IN）及其突变体表达为具有增强的绿色荧光蛋白的融合蛋白。通过荧光显微镜研究融合蛋白的亚细胞定位。发现 PFV IN 具有亲核性，并将融合蛋白靶向细胞核。突变分析表明，PFV IN 在其 C 端结构域中包含有效但不可转移的核定位信号 (NLS)，并在氨基酸 308 和 329 之间包含对其 NLS 功能至关重要的 5 个精氨酸和赖氨酸残基。
To analyse the potential karyophilic activity of prototype foamy viruses (PFVs), we expressed the PFV integrase (IN) and its mutants as fusion proteins with enhanced green fluorescence protein. The subcellular localization of the fusion proteins was investigated by fluorescence microscopy. The PFV IN was found to be karyophilic and targeted the fusion protein to the nucleus. Mutational analyses demonstrated that the PFV IN contains a potent but non-transferable nuclear localization signal (NLS) in its C-terminal domain and contains five arginine and lysine residues between amino acids 308 and 329 that are critical for its NLS function.