Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure

Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyc...

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Vydané v:	Nature (London) Ročník 544; číslo 7651; s. 440 - 445
Hlavní autori:	Liu, Xiaoyu, Li, Meijing, Xia, Xian, Li, Xueming, Chen, Zhucheng
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 27.04.2017 Nature Publishing Group
Predmet:	101/28 631/337/100/102 631/535/1258/1259 Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphatases - ultrastructure Amino Acid Sequence ATP Binding Sites Chromatin Chromatin Assembly and Disassembly Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism Enzymes Flexibility Histones - chemistry Histones - metabolism Humanities and Social Sciences Models, Molecular multidisciplinary Nucleosomes - chemistry Nucleosomes - metabolism Nucleosomes - ultrastructure Protein Binding Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Science Transcription Factors - chemistry Transcription Factors - metabolism Transcription Factors - ultrastructure
ISSN:	0028-0836, 1476-4687, 1476-4687
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