Preferred binding sites for [N-MeCys3,N-MeCys7]TANDEM determined using a universal footprinting substrate

被引：31

作者：

Lavesa, M ^{[1
]}

Fox, KR ^{[1
]}

机构：

[1] Univ Southampton, Sch Biol Sci, Div Biochem & Mol Biol, Southampton SO16 7PX, Hants, England

来源：

ANALYTICAL BIOCHEMISTRY | 2001年 / 293卷 / 02期

关键词：

footprinting; TANDEM; DNase I; quinoxaline antibiotic;

D O I：

10.1006/abio.2001.5124

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

We have prepared a novel footprinting substrate which contains all 136 tetranucleotide sequences and have used this to determine the preferred binding sites for the synthetic quinoxaline antibiotic [N-MeCys(3),N-MeCys(7)]TANDEM. We find that, although the ligand binds to all TpA steps, it binds best to the tetranucleotide sequence ATAT and shows only weak interaction with TTAA and G:TAC. The best binding sites contain the sequences ATAX and XTAT. (C) 2001 Academic Press.

引用

页码：246 / 250

页数：5

共 20 条

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