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

被引:314
作者
Hall, Michael A. [1 ]
Shundrovsky, Alla [1 ]
Bai, Lu [1 ]
Fulbright, Robert M. [1 ]
Lis, John T. [2 ]
Wang, Michelle D. [1 ,3 ]
机构
[1] Cornell Univ, Dept Phys, Atom & Solid State Phys Lab, Ithaca, NY 14853 USA
[2] Cornell Univ, Dept Mol Biol & Genet, Ithaca, NY 14853 USA
[3] Cornell Univ, Howard Hughes Med Inst, Ithaca, NY 14853 USA
基金
美国国家卫生研究院;
关键词
RNA-POLYMERASE-II; SINGLE CHROMATIN FIBERS; INDIVIDUAL NUCLEOSOMES; ANGSTROM RESOLUTION; CORE PARTICLE; TRANSCRIPTION; BARRIER; MOLECULES; REVEALS; FORCE;
D O I
10.1038/nsmb.1526
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
The nature of the nucleosomal barrier that regulates access to the underlying DNA during many cellular processes is not fully understood. Here we present a detailed map of histone-DNA interactions along the DNA sequence to near base pair accuracy by mechanically unzipping single molecules of DNA, each containing a single nucleosome. This interaction map revealed a distinct similar to 5-bp periodicity that was enveloped by three broad regions of strong interactions, with the strongest occurring at the dyad and the other two about +/- 40-bp from the dyad. Unzipping up to the dyad allowed recovery of a canonical nucleosome upon relaxation of the DNA, but unzipping beyond the dyad resulted in removal of the histone octamer from its initial DNA sequence. These findings have important implications for how RNA polymerase and other DNA-based enzymes may gain access to DNA associated with a nucleosome.
引用
收藏
页码:124 / 129
页数:6
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