Purification and characterization of ATBP, a novel protein that binds to A/T stretches in three segments of the Sarcophaga lectin gene.
Purification and characterization of ATBP, a novel protein that binds to A/T stretches in three segments of the Sarcophaga lectin gene.
复制标题
ATBP 的纯化和表征,ATBP 是一种与 Sarcophaga 凝集素基因的三个片段中的 A/T 片段结合的新型蛋白质。
DOI:
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发表时间:
1994
期刊:
影响因子:
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通讯作者:
Shunji Natori
中科院分区:
文献类型:
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作者:
Mayumi Matsui;Ayako Kobayashi;T. Kubo;Shunji Natori
A DNA-binding protein for the Sarcophaga lectin gene, ATBP (A/T-stretches-binding protein) was purified to homogeneity from the nuclear extract of NIH-Sape-4 cells. The molecular mass of ATBP determined under denaturing conditions was 53 kDa, but its native molecular mass estimated by gel-filtration chromatography was 430 kDa, suggesting that it is an octamer of the 53-kDa subunit. This protein bound to at least three DNA fragments from the Sarcophaga lectin gene, two of them are in the 5'-upstream region and the other is in a region containing an intron. These fragments are very AT rich and inlaid with stretches of A or T residues (A/T stretches). ATBP was found to have affinity for poly[d(A-T)]. These results suggest that ATBP binds to A/T stretches in the three DNA fragments from this gene. Furthermore, longer DNA was found to be bound more effectively, suggesting that an octamer of the 53-kDa subunit has multiple binding sites for the DNA fragments and requires a relatively long DNA sequence for binding.
影响因子:
56.9
作者:
BODE, J;KOHWI, Y;KOHWISHIGEMATSU, T
通讯作者:
KOHWISHIGEMATSU, T