Structural basis of nucleosome-dependent cGAS inhibition

Autor:	Andrew P. Cesmat, Robert K. McGinty, Qi Zhang, Cathy J. Spangler, Joshua D. Strauss, Pengda Liu, Joshua A. Boyer
Rok vydání:	2020
Předmět:	Multidisciplinary ATP synthase biology Chemistry Cryoelectron Microscopy Nuclear Proteins DNA Nucleotidyltransferases Article Nucleosomes Chromatin Cell biology chemistry.chemical_compound Cytosol medicine.anatomical_structure Catalytic Domain biology.protein medicine Humans Nucleosome Protein Multimerization Nuclear protein Cyclic guanosine monophosphate Nucleus
Zdroj:	Science
ISSN:	1095-9203 0036-8075
DOI:	10.1126/science.abd0609
Popis:	Saving a host cell from itself A fundamental mammalian defense mechanism against pathogens and damaged cellular DNA is to recognize DNA fragments in the cytosol and trigger an inflammatory response. The cyclic guanosine monophosphate–adenosine monophosphate synthase (cGAS) that recognizes cytosolic DNA is also found in the nucleus, but here its activity is suppressed by tethering to chromatin. Two papers now report cryo–electron microscopy structures of cGAS bound to the nucleosome core particle (NCP). Kujirai et al. observed a structure with two cGAS molecules bridging two NCPs, whereas Boyer et al. observed cGAS bound to a single nucleosome. Together, these structures show how cGAS is prevented from autoreactivity toward host DNA. Science , this issue p. 455 , p. 450
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29b04a141b630f7cdc72ca49af2639e5 https://doi.org/10.1126/science.abd0609 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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