Characterization of the HeLa cell 35 kDa Alu-element binding protein.
Characterization of the HeLa cell 35 kDa Alu-element binding protein.
复制标题
HeLa 细胞 35 kDa Alu 元件结合蛋白的表征。
DOI：
10.1007/bf00229310
复制
发表时间：
1996
影响因子：
4.3
通讯作者：
Vishwanatha,JK
中科院分区：
文献类型：
--
作者：
Chiang,Y;Vishwanatha,JK
humanu -elements是短的穿插DNA序列，约占人类基因组的5%。铝元素的生理作用尚不清楚，尽管它们被认为参与DNA复制，转录调控和信号识别颗粒RNA的核转运。在人类细胞中已经发现了与Alu-element和Alu RNA结合的蛋白质。在HeLa细胞中，两种分别为120 kDa和35 kDa的蛋白特异性结合铝元素。我们发现35 kDa蛋白只定位于细胞核，而120 kDa蛋白分布于细胞核和细胞质之间。35 kDa蛋白受磷酸化调节。去磷酸化后，其dna结合活性显著增强。与最近鉴定较小的铝元素结合蛋白为膜联蛋白11相反，我们发现膜联蛋白II不是铝元素结合蛋白。使用多种技术，我们证明了35 kDa的铝元素结合蛋白不同于膜联蛋白II。
HumanAlu-elements are short interspersed DNA sequences that comprise approximately 5% of the human genome. The physiological role of Alu-elements are unknown, although they are proposed to be involved in DNA replication, transcriptional regulation and nuclear transport of signal recognition particle RNA. Proteins that bind to Alu-element and Alu RNA have been identified in human cells. In HeLa cells, two proteins of 120 kDa and 35 kDa specifically bind to Alu-elements. We find that the 35 kDa protein is localized exclusively to the nucleus, while the 120 kDa protein is distributed between nucleus and cytoplasm. The 35 kDa protein is regulated by phosphorylation. Upon dephosphorylation, its DNA-binding activity is significantly enhanced. Contrary to the recent identification of the smaller Alu-element binding protein as annexin 11, we find that annexin II is not an Alu-element binding protein. Using a variety of techniques, we demonstrate that the 35 kDa Alu-element binding protein is distinct from annexin II.