首页> 美国卫生研究院文献>Nucleic Acids Research >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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Purification and molecular cloning of the scaffold attachment factor B (SAF-B) a novel human nuclear protein that specifically binds to S/MAR-DNA.

机译:支架附着因子B(SAF-B)的纯化和分子克隆SAF-B是一种特异性结合S / MAR-DNA的新型人类核蛋白。

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摘要

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.
机译:我们已经从HeLa细胞中纯化出近乎同质的新型核蛋白,该蛋白与支架或基质附着区DNA元件(S / MAR DNA)特异性结合。该蛋白被称为支架附着因子B的SAF-B,是染色质的丰富成分,但不是核基质的丰富成分,在所有研究的人体组织中均有表达。在兔体内产生了针对纯化蛋白的抗体,并通过免疫筛选用于分离编码SAF-B的完整cDNA。根据cDNA序列的预测,SAF-B包含849个氨基酸(96 696 Da),与任何已知蛋白均无显着同源性。 SAF-B富含带电残基,导致在SDS凝胶上异常迁移,并具有两个假定的二分核定位信号。

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