• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Set2-Dependent K36 Methylation Is Regulated by Novel Intratail Interactions within H3
【24h】

Set2-Dependent K36 Methylation Is Regulated by Novel Intratail Interactions within H3

机译：依赖Set2的K36甲基化受H3中新型尾部相互作用的调控

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

摘要

Posttranslational modifications to histones have been studied extensively, but the requirement for the residues within the tails for different stages of transcription is less clear. Using RNR3 as a model, we found that the residues within the N terminus of H3 are predominantly required for steps after transcription initiation and chromatin remodeling. Specifically, deleting as few as 20 amino acids, or substituting glutamines for lysines in the tail, greatly impaired K36 methylation by Set2. The mutations to the tail described here preserve the residues predicted to fill the active site of Set2, and the deletion mimics the recently described cleavage of the H3 tail that occurs during gene activation. Importantly, maintaining the charge of the unmodified tail by arginine substitutions preserves Set2 function in vivo. The H3 tail is dispensable for Set2 recruitment to genes but is required for the catalytic activity of Set2 in vitro. We propose that Set2 activity is controlled by novel intratail interactions which can be influenced by modifications and changes to the structure of the H3 tail to control the dynamics and localization of methylation during elongation.
机译：对组蛋白的翻译后修饰已经进行了广泛的研究，但是对于不同转录阶段的尾巴内残基的要求尚不清楚。使用 RNR3 作为模型，我们发现H3 N末端内的残基主要是转录起始和染色质重塑后的步骤所必需的。具体而言，删除少至20个氨基酸，或用谷氨酰胺代替尾巴中的赖氨酸，将大大损害Set2的K36甲基化。此处描述的尾巴突变保留了预计填充Set2活性位点的残基，该缺失模拟了基因激活过程中最近描述的H3尾巴裂解。重要的是，通过精氨酸取代维持未修饰尾巴的电荷可在体内保留Set2功能。 H3尾部对于Set2募集到基因是必不可少的，但对于Set2的体外催化活性是必需的。我们建议Set2活性是由新型尾内相互作用控制的，该相互作用可受到H3尾部结构的修饰和变化的影响，以控制延伸过程中甲基化的动力学和局部化。

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