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TitleStructural basis for nucleosome-mediated inhibition of cGAS activity.
Journal, issue, pagesCell Res, Vol. 30, Issue 12, Page 1088-1097, Year 2020
Publish dateOct 13, 2020
AuthorsDuanfang Cao / Xiaonan Han / Xiaoyi Fan / Rui-Ming Xu / Xinzheng Zhang /
PubMed AbstractActivation of cyclic GMP-AMP synthase (cGAS) through sensing cytosolic double stranded DNA (dsDNA) plays a pivotal role in innate immunity against exogenous infection as well as cellular regulation ...Activation of cyclic GMP-AMP synthase (cGAS) through sensing cytosolic double stranded DNA (dsDNA) plays a pivotal role in innate immunity against exogenous infection as well as cellular regulation under stress. Aberrant activation of cGAS induced by self-DNA is related to autoimmune diseases. cGAS accumulates at chromosomes during mitosis or spontaneously in the nucleus. Binding of cGAS to the nucleosome competitively attenuates the dsDNA-mediated cGAS activation, but the molecular mechanism of the attenuation is still poorly understood. Here, we report two cryo-electron microscopy structures of cGAS-nucleosome complexes. The structures reveal that cGAS interacts with the nucleosome as a monomer, forming 1:1 and 2:2 complexes, respectively. cGAS contacts the nucleosomal acidic patch formed by the H2A-H2B heterodimer through the dsDNA-binding site B in both complexes, and could interact with the DNA from the other symmetrically placed nucleosome via the dsDNA-binding site C in the 2:2 complex. The bound nucleosome inhibits the activation of cGAS through blocking the interaction of cGAS with ligand dsDNA and disrupting cGAS dimerization. R236A or R255A mutation of cGAS impairs the binding between cGAS and the nucleosome, and largely relieves the nucleosome-mediated inhibition of cGAS activity. Our study provides structural insights into the inhibition of cGAS activity by the nucleosome, and advances the understanding of the mechanism by which hosts avoid the autoimmune attack caused by cGAS.
External linksCell Res / PubMed:33051594 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.9 Å
Structure data

30339

7ccq

EMDB-30339, PDB-7ccq:
Structure of the 1:1 cGAS-nucleosome complex
Method: EM (single particle) / Resolution: 3.8 Å

30340

7ccr

EMDB-30340, PDB-7ccr:
Structure of the 2:2 cGAS-nucleosome complex
Method: EM (single particle) / Resolution: 4.9 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN/TRANSFERASE/DNA / cGAS / nucleosome / inhibition / cryo-EM / IMMUNE SYSTEM / STRUCTURAL PROTEIN-TRANSFERASE-DNA complex

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