IDENTIFICATION OF THE NUCLEOLAR TARGETING SIGNAL OF HUMAN ANGIOGENIN
IDENTIFICATION OF THE NUCLEOLAR TARGETING SIGNAL OF HUMAN ANGIOGENIN
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DOI：
10.1006/bbrc.1994.2391
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发表时间：
1994-09-30
影响因子：
3.1
通讯作者：
RIORDAN, JF
中科院分区：
文献类型：
--
作者：
MOROIANU, J;RIORDAN, JF
血管生成素被亚融合的内皮细胞内吞，易位到细胞核并积聚在核仁中。它还定位于毛地黄皂苷透化的内皮细胞的核仁中。对应于人血管生成素的残基31-35的肽RRRGL特异性地将非核载体蛋白如白蛋白、抗人核仁单克隆抗体和R33 A血管生成素靶向透化内皮细胞的核仁。与“突变”肽RRAGL结合的蛋白质不进口。异硫氰酸黄绿素结合的RRRGL也迅速输入细胞核并定位于核仁，而“突变体"肽则不然。残基R33是核转位所必需的，R31和R32似乎调节这一过程。因此，（31）RRRGL（35）是负责人血管生成素的核仁靶向的核定位信号。(C)1994年出版社出版。
Angiogenin is endocytosed by subconfluent endothelial cells, translocated to the nucleus and accumulates in the nucleolus. It also localizes into the nucleolus of digitonin-permeabilized endothelial cells. The peptide RRRGL corresponding to residues 31-35 of human angiogenin specifically targets non-nuclear carrier proteins such as albumin, an anti-human nucleolus monoclonal antibody and R33A angiogenin to the nucleolus of permeabilized endothelial cells. Proteins conjugated with a ''mutant'' peptide, RRAGL, are not imported. Fluorescein isothiocyanate-conjugated RRRGL is also rapidly imported into the nucleus and localized to the nucleolus, whereas the ''mutant'' peptide is not. Residue R33 is essential for nuclear translocation and R31 and R32 appear to modulate this process. Thus, (31)RRRGL(35) is a nuclear localization signal responsible for the nucleolar targeting of human angiogenin. (C) 1994 Academic Press, Inc.