HISTONE-H1 INHIBITS EUKARYOTIC DNA TOPOISOMERASE-I

被引：13

作者：

RICHTER, A

KAPITZA, M

机构：

[1] Division of Biology, University of Konstanz

来源：

FEBS LETTERS | 1991年 / 294卷 / 1-2期

关键词：

TOPOISOMERASE-I; RELAXATION; CLEAVAGE; HISTONE-H1;

D O I：

10.1016/0014-5793(91)81357-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Histone H1 inhibits the catalytic activity of topoisomerase I in vitro. The relaxation activity of the enzyme is partially inhibited at a molar ratio of one histone H1 molecule per 40 base pairs (bp) of DNA and completely inhibited at a molar ratio of one histone H1 molecule per 10 base pairs of DNA. Increasing the amount of enzyme at a constant histone H1 to DNA ratio antagonizes the inhibition. This indicates that topoisomerase I and histone H1 compete for binding sites on the substrate DNA molecules. Consistent with this we show on the sequence level that histone H1 inhibits the cleavage reaction of topoisomerase I on linear DNA fragments.

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页码：125 / 128

页数：4

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