Literature DB >> 15965484

Splicing regulates NAD metabolite binding to histone macroH2A.

Georg Kustatscher1, Michael Hothorn, Céline Pugieux, Klaus Scheffzek, Andreas G Ladurner.   

Abstract

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-A 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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Year:  2005        PMID： 15965484     DOI： 10.1038/nsmb956

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN： 1545-9985            Impact factor:   15.369


  145 in total

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Review 9.  Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation.

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10.  Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose.

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Journal:  Anal Biochem       Date:  2008-09-07       Impact factor: 3.365
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