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Sci Rep:上海交通大学陈海峰研究组等发表组蛋白协同修饰研究进展

摘要 : 2016年4月15日,国际学术权威刊物自然出版集团旗下子刊《Scientific Reports》在线发表了上海交通大学生命科学技术学院陈海峰研究团队以及加州大学尔湾分校Ray Luo研究员合作的文章。

 2016年4月15日,国际学术权威刊物自然出版集团旗下子刊《Scientific Reports》在线发表了上海交通大学生命科学技术学院陈海峰研究团队以及加州大学尔湾分校Ray Luo研究员合作的文章,文章题为“Synergistic Modification Induced Specific Recognition between Histone and TRIM24 via Fluctuation Correlation Network Analysis”。该研究首次采用动态相关网络分析的方法研究了组蛋白协同修饰与TRIM24蛋白的特异性识别。

组蛋白可以发生甲基化、乙酰化、磷酸化、泛素化等不同的修饰,从而调控基因的表达;不同的组蛋白修饰能够被对应的组蛋白“reader”识别和结合,然而这些蛋白是如何特异识别特定类型的组蛋白修饰,目前的研究还尚不清楚。

研究利用分子动力学模拟结合动态网络分析的方法,通过构建不同的组蛋白修饰体系,系统的分析了与乳腺癌相关的“reader”蛋白TRIM24与组蛋白修饰的关系。研究发现TRIM24蛋白在结合不同位点和不同类型的组蛋白修饰后构象和蛋白内部网络存在差异显著,在动态网络以及社区网络分类的基础上提出了“协同修饰诱导识别”的理论,对于靶向“reader”蛋白的药物发现具有重要的指导意义。同时,这一方法对于生物大分子间的别构以及信号传导等机制的研究也具有重要意义。

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图:组蛋白协同修饰

原文链接:

Synergistic Modification Induced Specific Recognition between Histone and TRIM24 viaFluctuation Correlation Network Analysis

原文摘要:

Histone modification plays a key role in gene regulation and gene expression. TRIM24 as a histone reader can recognize histone modification. However the specific recognition mechanism between TRIM24 and histone modification is unsolved. Here, systems biology method of dynamics correlation network based on molecular dynamics simulation was used to answer the question. Our network analysis shows that the dynamics correlation network of H3K23ac is distinctly different from that of wild type and other modifications. A hypothesis of “synergistic modification induced recognition” is then proposed to link histone modification and TRIM24 binding. These observations were further confirmed from community analysis of networks with mutation and network perturbation. Finally, a possible recognition pathway is also identified based on the shortest path search for H3K23ac. Significant difference of recognition pathway was found among different systems due to methylation and acetylation modifications. The analysis presented here and other studies show that the dynamic network-based analysis might be a useful general strategy to study the biology of protein post-translational modification and associated recognition.

来源: Scientific Reports 浏览次数:0

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