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Splicing regulates NAD metabolite binding to histone macroH2A.

Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG
Nat Struct Mol Biol 12 624-5 (2005)
Cited: 209 times
EuropePMC logo PMID: 15965484

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.

Reviews - 2fxk mentioned but not cited (2)

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Articles - 2fxk mentioned but not cited (4)

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