Simos G, Georgatos S D
Programme of Cell Biology, European Molecular Biology Laboratory, Heidelberg, Germany.
FEBS Lett. 1994 Jun 13;346(2-3):225-8. doi: 10.1016/0014-5793(94)00479-x.
The lamin B receptor (p58) is an inner nuclear membrane protein that forms an in vivo complex with the nuclear lamins, a nuclear envelope kinase, and two other nuclear proteins with apparent M(r) of 18,000 (p18) and 34,000 (p34). We now report the isolation of p34 by partial dissociation of the immunoaffinity-purified p58 protein complex. Determination of the N-terminal amino acid sequence of purified p34 shows that this polypeptide is homologous to p32, a splicing factor 2 (SF2)-associated protein. The relatedness between p34 and p32 can be further established by showing that antibodies raised against N- and C-terminal peptides of p32 cross-react with purified p34. As the amino acid sequence of p58 contains an arginine/serine (RS)-rich region similar to the RS-rich region found in SF 2, we speculate that these domains provide binding sites for p34 and that this protein may be a linker between the nuclear membrane and intranuclear spliceosomal substructures.
核纤层蛋白B受体（p58）是一种内核膜蛋白，它在体内与核纤层蛋白、一种核膜激酶以及另外两种表观分子量分别为18,000（p18）和34,000（p34）的核蛋白形成复合物。我们现在报告通过免疫亲和纯化的p58蛋白复合物的部分解离来分离p34。对纯化的p34的N端氨基酸序列的测定表明，该多肽与p32同源，p32是一种与剪接因子2（SF2）相关的蛋白。通过显示针对p32的N端和C端肽产生的抗体与纯化的p34交叉反应，可以进一步确定p34与p32之间的相关性。由于p58的氨基酸序列包含一个富含精氨酸/丝氨酸（RS）的区域，类似于在SF2中发现的富含RS的区域，我们推测这些结构域为p34提供了结合位点，并且该蛋白可能是核膜与核内剪接体亚结构之间的连接物。
