Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA
Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA
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DOI：
10.1093/nar/24.5.843
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发表时间：
1996-03-01
影响因子：
14.9
通讯作者：
Fackelmayer, FO
中科院分区：
文献类型：
--
作者：
Renz, A;Fackelmayer, FO
我们已经从HeLa细胞中纯化出一种接近同质性的新型核蛋白，该蛋白特异性结合支架或基质附着区DNA元件（S/MAR DNA），该蛋白被命名为支架附着因子B的SAF-B，是染色质的丰富成分，但不属于核基质，并且在所有研究的人类组织中表达。根据cDNA序列预测，SAF-B含有849个氨基酸（96 696 Da），与任何已知蛋白无显著同源性，SAF-B富含带电残基，导致在SDS凝胶上的异常迁移，并具有两个推测的双部核定位信号。
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.