Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding
Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding
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DOI：
10.1073/pnas.95.9.4947
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发表时间：
1998-04-28
影响因子：
11.1
通讯作者：
Workman, JL
中科院分区：
文献类型：
--
作者：
Côté, J;Peterson, CL;Workman, JL
为了研究SWI/SNF的作用机制，我们分析了SWI/SNF刺激转录因子结合核小体核心复合物形成的途径。我们在这里报道，SWI/SNF复合物直接结合核小体核心，并利用ATP水解的能量破坏组蛋白/DNA相互作用，改变DNA在组蛋白八聚体周围弯曲的首选路径。这种破坏发生在没有将DNA与组蛋白八聚体表面分离的情况下，SWI/SNF对核小体DNA的atp依赖性破坏会产生核小体核心构象的改变，这种改变可以在SWI/SNF复合物分离后持续很长一段时间。这种被破坏的构象保留了对转录因子GAL4-AH的增强亲和力。因此，atp依赖的核小体核心破坏和转录因子的增强结合可以暂时分开。这些结果表明，SWI/SNF可以在转录因子相互作用之前短暂地参与染色质结构的重塑。
To investigate the mechanism of SWI/SNF action, we have analyzed the pathway by which SWI/SNF stimulates formation of transcription factor-bound nucleosome core complexes. We report here that the SWI/SNF complex binds directly to nucleosome cores and uses the energy of ATP hydrolysis to disrupt histone/DNA interactions, altering the preferred path of DNA bending around the histone octamer. This disruption occurs without dissociating the DNA from the surface of the histone octamer, ATP-dependent disruption of nucleosomal DNA by SWI/SNF generates an altered nucleosome core conformation that can persist for an extended period after detachment of the SWI/SNF complex. This disrupted conformation retains an enhanced affinity for the transcription factor GAL4-AH. Thus, ATP-dependent nucleosome core disruption and enhanced binding of the transcription factor can be temporally separated. These results indicate that SWI/SNF can act transiently in the remodeling of chromatin structure, even before interactions of transcription factors.