Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome binding

The eukaryotic genome is packed into highly compacted chromatin, the basic unit of which is a nucleo- some composed of 147 base pairs of DNA wrapped around the histone octamer. Post-translational modifications along histone N-terminal tails can be recognized by various ＇reader＇ modules . PWWP domain...

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Veröffentlicht in:	Cell research 2014-07, Vol.24 (7), p.890-893
Hauptverfasser:	Wang, Juncheng, Qin, Su, Li, Fudong, Li, Sai, Zhang, Wei, Peng, Junhui, Zhang, Zhiyong, Gong, Qingguo, Wu, Jihui, Shi, Yunyu
Format:	Artikel
Sprache:	eng
Schlagworte:	631/337 631/45/535 Carrier Proteins - chemistry Carrier Proteins - metabolism Cell Biology Crystallography, X-Ray Histones - metabolism Humans Letter to the Editor Life Sciences Methylation Models, Molecular Nucleosomes - metabolism Protein Structure, Tertiary Zinc Fingers 人类基本单元晶体结构染色质核基因组溴组蛋白翻译后修饰
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Beschreibung
Zusammenfassung:	The eukaryotic genome is packed into highly compacted chromatin, the basic unit of which is a nucleo- some composed of 147 base pairs of DNA wrapped around the histone octamer. Post-translational modifications along histone N-terminal tails can be recognized by various ＇reader＇ modules . PWWP domain, one type of ＇reader＇ modules, has been identified to recognize H3K36me3 in the peptide and nucleosome context .
ISSN:	1001-0602 1748-7838
DOI:	10.1038/cr.2014.38