Human topoisomerase II-DNA interaction study by using atomic force microscopy

被引：23

作者：

Alonso-Sarduy, Livan ^{[1
]}

Roduit, Charles ^{[1
]}

Dietler, Giovanni ^{[1
]}

Kasas, Sandor ^{[1
,2
]}

机构：

[1] Ecole Polytech Fed Lausanne, Lab Phys Mat Vivante, CH-1015 Lausanne, Switzerland

[2] Univ Lausanne UNIL, Dept Biol Cellulaire & Morphol, CH-1015 Lausanne, Switzerland

来源：

FEBS LETTERS | 2011年 / 585卷 / 19期

基金：

瑞士国家科学基金会;

关键词：

AFM; DNA topology; Human topoisomerase II; Binding geometry; Time-lapse imaging; Protein-DNA interaction; POSITIVELY SUPERCOILED DNA; MECHANISM; TOPOLOGY; CLEAVAGE; IV; SIMPLIFICATION; PROVIDES; BINDING;

D O I：

10.1016/j.febslet.2011.08.051

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Type II topoisomerases (Topo II) are unique enzymes that change the DNA topology by catalyzing the passage of two double-strands across each other by using the energy from ATP hydrolysis. In vitro, human Topo II relaxes positive supercoiled DNA around 10-fold faster than negative supercoiled DNA. By using atomic force microscopy (AFM) we found that human Topo II binds preferentially to DNA cross-overs. Around 50% of the DNA crossings, where Topo II was bound to, presented an angle in the range of 80-90 degrees, suggesting a favored binding geometry in the chiral discrimination by Topo II. Our studies with AFM also helped us visualize the dynamics of the unknotting action of Topo II in knotted molecules. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3139 / 3145

页数：7

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