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Computational study of associations between histone modification and protein-DNA binding in yeast genome by integrating diverse information

机译:通过整合各种信息对酵母基因组中组蛋白修饰与蛋白质-DNA结合的关联进行计算研究

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Background In parallel with the quick development of high-throughput technologies, in vivo (vitro) experiments for genome-wide identification of protein-DNA interactions have been developed. Nevertheless, a few questions remain in the field, such as how to distinguish true protein-DNA binding (functional binding) from non-specific protein-DNA binding (non-functional binding). Previous researches tackled the problem by integrated analysis of multiple available sources. However, few systematic studies have been carried out to examine the possible relationships between histone modification and protein-DNA binding. Here this issue was investigated by using publicly available histone modification data in yeast. Results Two separate histone modification datasets were studied, at both the open reading frame (ORF) and the promoter region of binding targets for 37 yeast transcription factors. Both results revealed a distinct histone modification pattern between the functional protein-DNA binding sites and non-functional ones for almost half of all TFs tested. Such difference is much stronger at the ORF than at the promoter region. In addition, a protein-histone modification interaction pathway can only be inferred from the functional protein binding targets. Conclusions Overall, the results suggest that histone modification information can be used to distinguish the functional protein-DNA binding from the non-functional, and that the regulation of various proteins is controlled by the modification of different histone lysines such as the protein-specific histone modification levels.
机译:背景技术与高通量技术的快速发展并行,已经开发了用于蛋白质-DNA相互作用的全基因组鉴定的体内(体外)实验。然而,该领域仍存在一些问题,例如如何区分真正的蛋白质-DNA结合(功能性结合)与非特异性蛋白质-DNA结合(非功能性结合)。以前的研究通过对多个可用来源的综合分析解决了该问题。但是,很少有系统的研究来检查组蛋白修饰和蛋白质-DNA结合之间的可能关系。在这里,此问题是通过使用酵母中公开可用的组蛋白修饰数据进行调查的。结果研究了两个独立的组蛋白修饰数据集,分别位于开放阅读框(ORF)和37个酵母转录因子结合靶标的启动子区域。两项结果均显示,在几乎所有测试的TF中,功能性蛋白质-DNA结合位点和非功能性结合位点之间存在明显的组蛋白修饰模式。这种差异在ORF处比在启动子区要强得多。另外,只能从功能性蛋白质结合靶标推断出蛋白质-组蛋白修饰相互作用途径。结论总体而言,结果表明,组蛋白修饰信息可用于区分功能性蛋白质与DNA的结合与非功能性结合,并且各种蛋白质的调节受不同组蛋白赖氨酸(例如蛋白质特异性组蛋白)的修饰控制修改级别。

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