• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Epigenetics & Chromatin >Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3
【24h】

Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3

机译：组蛋白H3球状结构域内关键残基对伴侣结合和核小体动力学的调节

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Background Nucleosomes have an important role in modulating access of DNA by regulatory factors. The role specific histone residues have in this process has been shown to be an important mechanism of transcription regulation. Previously, we identified eight amino acids in histones H3 and H4 that are required for nucleosome occupancy over highly transcribed regions of the genome. Results We investigate the mechanism through which three of these previously identified histone H3 amino acids regulate nucleosome architecture. We find that histone H3 K122, Q120, and R49 are required for Spt2, Spt6, and Spt16 occupancies at genomic locations where transcription rates are high, but not over regions of low transcription rates. Furthermore, substitution at one residue, K122, located on the dyad axis of the nucleosome, results in improper reassembly and disassembly of nucleosomes, likely accounting for the transcription rate-dependent regulation by these mutant histones. Conclusions These data show that when specific amino acids of histone proteins are substituted, Spt2, Spt6, and Spt16 occupancies are reduced and nucleosome dynamics are altered. Therefore, these data support a mechanism for histone chaperone binding where these factors interact with histone proteins to promote their activities during transcription.
机译：背景技术核小体在调节因子调节DNA的进入中具有重要作用。特定的组蛋白残基在此过程中的作用已被证明是转录调节的重要机制。以前，我们在组蛋白H3和H4中确定了在基因组高度转录区域中核小体占据所需的8个氨基酸。结果我们研究了其中三个先前鉴定出的组蛋白H3氨基酸调节核小体结构的机制。我们发现组蛋白H3 K122，Q120和R49是在转录率高的基因组位置（而不是在转录率低的区域）占据Spt2，Spt6和Spt16所必需的。此外，在位于核小体的二元轴上的一个残基K122处的取代导致核小体的不正确重组和解体，这很可能解释了这些突变组蛋白的转录速率依赖性调节。结论这些数据表明，当组蛋白的特定氨基酸被取代时，Spt2，Spt6和Spt16的占有率降低，核小体动力学改变。因此，这些数据支持了组蛋白伴侣结合的机制，其中这些因素与组蛋白相互作用，从而在转录过程中促进其活性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号