Splicing regulates NAD metabolite binding to histone macroH2A

被引：244

作者：

Kustatscher, G

Hothorn, M

Pugieux, C

Scheffzek, K

Ladurner, AG

机构：

[1] European Mol Biol Lab, Gene Express Unit, D-69117 Heidelberg, Germany

[2] European Mol Biol Lab, Computat Biol Unit, D-69117 Heidelberg, Germany

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 07期

关键词：

D O I：

10.1038/nsmb956

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show that human macroH2A1.1 binds the SirT1-metabolite O-acetyl-ADP-ribose (OAADPR) through its macro domain. The 1.6-angstrom crystal structure and mutants reveal how the metabolite is recognized. Mutually exclusive exon use in the gene H2AFY produces macroH2A1.2, whose tissue distribution differs. MacroH2A1.2 shows only subtle structural changes but cannot bind nucleotides. Alternative splicing may thus regulate the binding of nicotinamide adenine dinucleotide (NAD) metabolites to chromatin.

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收藏

页码：624 / 625

页数：2

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