Splicing regulates NAD metabolite binding to histone macroH2A

@article{Kustatscher2005SplicingRN,
  title={Splicing regulates NAD metabolite binding to histone macroH2A},
  author={Georg Kustatscher and Michael Hothorn and C{\'e}line Pugieux and Klaus Scheffzek and Andreas G Ladurner},
  journal={Nature Structural &Molecular Biology},
  year={2005},
  volume={12},
  pages={624-625}
}
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-Å 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… CONTINUE READING
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