Nuclear and nucleolar targeting of human ribosomal protein S6.
Nuclear and nucleolar targeting of human ribosomal protein S6.
复制标题
人核糖体蛋白 S6 的核和核仁靶向。
DOI：
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发表时间：
1995
影响因子：
3.3
通讯作者：
Joachim Kruppa
中科院分区：
文献类型：
--
作者：
Carola Schmidt;Edgar Lipsius;Joachim Kruppa
构建嵌合蛋白以定义人核糖体蛋白S6的核定位信号（NLS）。利用重组技术将人核糖体蛋白S6的完整cDNA序列、不同的cDNA片段和寡核苷酸分别连接到大肠杆菌LacZ基因的5 ′端。将杂交基因转染到L细胞中，瞬时表达，并通过其β-半乳糖苷酶活性确定融合蛋白的细胞内定位。在S6蛋白的C-末端的一半中鉴定了三个NLS。缺失诱变证明，单个NLS足以将相应的S6-β-半乳糖苷酶嵌合体靶向到细胞核中。去除所有三个假定的NLS完全阻断了所得S6-β-半乳糖苷酶融合蛋白的核输入，而不是均匀分布在细胞质中。含有S6缺失突变体和至少一个单一NLS或未修饰的S6的嵌合体在核仁中积累。几个结构的分析揭示了存在一个特定的结构域，这是必不可少的，但不足以核仁积累的S6。
Chimeric proteins were constructed to define the nuclear localization signals (NLSs) of human ribosomal protein S6. The complete cDNA sequence, different cDNA fragments and oligonucleotides of the human ribosomal proteins S6, respectively, were joined to the 5' end of the entire LacZ gene of Escherichia coli by using recombinant techniques. The hybrid genes were transfected into L cells, transiently expressed, and the intracellular location of the fusion proteins was determined by their beta-galactosidase activity. Three NLSs were identified in the C-terminal half of the S6 protein. Deletion mutagenesis demonstrated that a single NLS is sufficient for targeting the corresponding S6-beta-galactosidase chimera into the nucleus. Removal of all three putative NLSs completely blocked the nuclear import of the resulting S6-beta-galactosidase fusion protein, which instead became evenly distributed in the cytoplasm. Chimeras containing deletion mutants of S6 with at least one single NLS or unmodified S6 accumulated in the nucleolus. Analysis of several constructs reveals the existence of a specific domain that is essential but not sufficient for nucleolar accumulation of S6.
远端蛋白质序列可以影响核定位信号的功能。
影响因子：
5.3
作者：
Gao,M;Knipe,DM
通讯作者：
Knipe,DM
大鼠核糖体蛋白S6的一级结构。
DOI：
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发表时间：
1988
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Chan,YL;Wool,IG
通讯作者：
Wool,IG