High-resolution dynamic mapping of histone-DNA interactions in a nucleosome

被引：0
|
作者：
Michael A Hall
Alla Shundrovsky
Lu Bai
Robert M Fulbright
John T Lis
Michelle D Wang
机构：
[1] Cornell University,Department of Physics—Laboratory of Atomic and Solid State Physics
[2] Cornell University,Department of Molecular Biology and Genetics
[3] Howard Hughes Medical Institute,undefined
[4] Cornell University,undefined
[5] Present addresses: Department of Mechanical Engineering,undefined
[6] Yale University,undefined
[7] New Haven,undefined
[8] Connecticut 06511,undefined
[9] USA (A.S.); Rockefeller University,undefined
[10] 1230 York Avenue,undefined
[11] New York,undefined
[12] New York 10065,undefined
[13] USA (L.B.).,undefined
来源：
Nature Structural & Molecular Biology | 2009年 / 16卷
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学科分类号：
摘要：
DNA packaging into nucleosomes presents a barrier to many motor proteins, including the transcriptional machinery. By unzipping DNA in single nucleosomes, a detailed map at near base pair resolution of histone-DNA interactions is now provided, suggesting that interaction with the two DNA strands is decoupled and that unraveling past the dyad axis of the nucleosome, as might occur when a motor protein passes through, is sufficient to displace histones.
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页码：124 / 129
页数：5
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