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TitleStructural basis for the inhibition of cGAS by nucleosomes.
Journal, issue, pagesScience, Year 2020
Publish dateSep 10, 2020
AuthorsTomoya Kujirai / Christian Zierhut / Yoshimasa Takizawa / Ryan Kim / Lumi Negishi / Nobuki Uruma / Seiya Hirai / Hironori Funabiki / Hitoshi Kurumizaka /
PubMed AbstractThe cyclic GMP-AMP synthase (cGAS) senses invasion of pathogenic DNA and stimulates inflammatory signaling, autophagy and apoptosis. Organization of host DNA into nucleosomes was proposed to limit ...The cyclic GMP-AMP synthase (cGAS) senses invasion of pathogenic DNA and stimulates inflammatory signaling, autophagy and apoptosis. Organization of host DNA into nucleosomes was proposed to limit cGAS autoinduction, but the underlying mechanism was unknown. Here, we report the structural basis for this inhibition. In the cryo-EM structure of the human cGAS-nucleosome core particle (NCP) complex, two cGAS monomers bridge two NCPs by binding the acidic patch of H2A-H2B and nucleosomal DNA. In this configuration, all three known cGAS DNA-binding sites, required for cGAS activation, are repurposed or become inaccessible, and cGAS dimerization, another prerequisite for activation, is inhibited. Mutating key residues linking cGAS and the acidic patch alleviates nucleosomal inhibition. This study establishes a structural framework for why cGAS is silenced on chromatinized self-DNA.
External linksPubMed:32912999 / Publisher's page
KeywordsDNA BINDING PROTEIN/DNA / complex / chromatin / NTase / innate immunity / immunity / nucleosome / cGAS / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex
MethodsEM (single particle)
Resolution3.9 A
Structure data

EMDB-30267:
Human cGAS-nucleosome complex

PDB-7c0m:
Human cGAS-nucleosome complex

Chemicals

ChemComp-ZN:
ZINC ION / Zinc

Source
  • homo sapiens (human)
  • synthetic construct (others)

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