Renz A, Fackelmayer F O
Division of Biology, University of Konstanz, Germany.
Nucleic Acids Res. 1996 Mar 1;24(5):843-9. doi: 10.1093/nar/24.5.843.
We have purified to near homogeneity a novel nuclear protein from HeLa cells, that specifically binds to scaffold or matrix attachment region DNA elements (S/MAR DNA). The protein, designated SAF-B for scaffold attachment factor B, is an abundant component of chromatin, but not of the nuclear matrix and is expressed in all human tissues investigated. Antibodies against the purified protein were raised in rabbit and used to isolate the complete cDNA encoding SAF-B by immunoscreening. As predicted from the cDNA sequence, SAF-B contains 849 amino acids (96 696 Da), without significant homology to any known protein. SAF-B is rich in charged residues, leading to an aberrant migration on SDS gels, and has two putative bipartite nuclear localisation signals.
我们已从HeLa细胞中纯化出一种新型核蛋白，其能特异性结合支架或基质附着区域DNA元件（S/MAR DNA）。该蛋白被命名为支架附着因子B（SAF-B），是染色质的丰富组成成分，但不是核基质的组成成分，且在所研究的所有人类组织中均有表达。针对纯化蛋白制备了兔抗体，并通过免疫筛选用于分离编码SAF-B的完整cDNA。根据cDNA序列预测，SAF-B含有849个氨基酸（96 696 Da），与任何已知蛋白均无明显同源性。SAF-B富含带电荷的残基，导致其在SDS凝胶上出现异常迁移，并且有两个假定的双分型核定位信号。
