Novobiocin precipitates histones at concentrations normally used to inhibit eukaryotic type II topoisomerase.
Novobiocin precipitates histones at concentrations normally used to inhibit eukaryotic type II topoisomerase.
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新生霉素以通常用于抑制真核 II 型拓扑异构酶的浓度沉淀组蛋白。
DOI：
10.1093/nar/14.9.3671
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发表时间：
1986
影响因子：
14.9
通讯作者：
Chalkley,R
中科院分区：
文献类型：
--
作者：
Cotten,M;Bresnahan,D;Thompson,S;Sealy,L;Chalkley,R
在通常用于抑制真核II型拓扑异构酶活性的浓度（100-1000 μg/ml）下，新生霉素结合核心组蛋白。每摩尔组蛋白结合约15摩尔新生霉素，导致组蛋白从0.15 M或2 M NaCl溶液中沉淀。新生霉素和蛋白质之间的相互作用似乎涉及精氨酸残基：组蛋白H3和H4（13.5和14摩尔%精氨酸）在低于组蛋白H2 A和H2 B（9.5和6.5摩尔%精氨酸）的新生霉素浓度下沉淀。此外，聚精氨酸而不是聚鸟氨酸在组蛋白沉淀中竞争新生霉素。此外，具有用1，2-环己二酮修饰的精氨酸残基的组蛋白可溶于1000 μg/ml新生霉素。因为新生霉素可以从溶液中除去组蛋白以及抑制拓扑异构酶活性，并且因为这两种事件都可以改变DNA拓扑结构，所以在设计用于暗示染色质动力学中的拓扑异构酶活性的实验中应谨慎使用新生霉素。
At concentrations normally used to inhibit eukaryotic type II topoisomerase activity (100–1000 μg/ml) novobiocin binds core histones. Approximately 15 moles of novobiocin bind per mole of histone resulting in histone precipitation from solution in either 0.15 M or 2 M NaCl. The interaction between novobiocin and proteins appears to involve arginine residues: histones H3 and H4 (13.5 and 14 mole percent arginine) are precipitated at lower novobiocin concentrations than histones H2A and H2B (9.5 and 6.5 mole percent arginine). Furthermore, polyarginine but not polyornithine competes for novobiocin in histone precipitation. Moreover, histones with arginine residues modified with 1,2-cyclohexanedione are soluble in 1000 μg/ml novobiocin. Because novobiocin can remove histones from solution as well as inhibit topoisomerase activity, and because both of these events can alter DNA topology, novobiocin should be used with caution in experiments designed to implicate topoisomerase activity in chromatin dynamics.