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TitleStructural basis of nucleosome-dependent cGAS inhibition.
Journal, issue, pagesScience, Year 2020
Publish dateSep 10, 2020
AuthorsJoshua A Boyer / Cathy J Spangler / Joshua D Strauss / Andrew P Cesmat / Pengda Liu / Robert K McGinty / Qi Zhang /
PubMed AbstractCyclic GMP-AMP synthase (cGAS) recognizes cytosolic foreign or damaged DNA to activate the innate immune response to infection, inflammatory diseases, and cancer. In contrast, cGAS reactivity against ...Cyclic GMP-AMP synthase (cGAS) recognizes cytosolic foreign or damaged DNA to activate the innate immune response to infection, inflammatory diseases, and cancer. In contrast, cGAS reactivity against self-DNA in the nucleus is suppressed by chromatin tethering. We report a 3.3-angstrom-resolution cryo-electron microscopy structure of cGAS in complex with the nucleosome core particle. The structure reveals that cGAS employs two conserved arginines to anchor to the nucleosome acidic patch. The nucleosome binding interface exclusively occupies the strong dsDNA binding surface on cGAS and sterically prevents cGAS from oligomerizing into the functionally active 2:2 cGAS-dsDNA state. These findings provide a structural basis for how cGAS maintains an inhibited state in the nucleus and further exemplify the role of the nucleosome in regulating diverse nuclear protein functions.
External linksPubMed:32913000 / Publisher's page
KeywordsDNA Binding Protein/DNA/Transferase / cGAS / nucleosome / cyclic GMP-AMP synthase / DNA Binding Protein-DNA-Transferase complex
MethodsEM (single particle)
Resolution3.3 - 3.9 A
Structure data

EMDB-22408:
1:1 cGAS-nucleosome complex

EMDB-22409:
2:1 cGAS-nucleosome complex

EMDB-22413:
1:1 cGAS(mask)-NCP map

PDB-7jo9:
1:1 cGAS-nucleosome complex

PDB-7joa:
2:1 cGAS-nucleosome complex

Chemicals

ChemComp-ZN:
ZINC ION / Zinc

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • mus musculus (house mouse)

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