The N terminus of cGAS de-oligomerizes the cGAS: DNA complex and lifts the DNA size restriction of core-cGAS activity

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Cyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme in the innate immune system. Recent studies using core-cGAS lacking the N terminus investigated the mechanism for binding of double-stranded (ds) DNA and synthesis of 2 ',3 '-cyclic GMP-AMP (cGAMP), a secondary messenger that ultimately induces type I interferons. However, the function of the N terminus of cGAS remains largely unknown. Here, we found that the N terminus enhanced the activity of core-cGAS in vivo. Importantly, the catalytic activity of core-cGAS decreased as the length of double-stranded DNA (dsDNA) increased, but the diminished activity was restored by addition of the N terminus. Furthermore, the N terminus de-oligomerized the 2 : 2 complex of core-cGAS and dsDNA into a 1 : 1 complex, suggesting that the N terminus enhanced the activity of core-cGAS by facilitating formation of a monomeric complex of cGAS and DNA.
Publisher
WILEY
Issue Date
2017-03
Language
English
Article Type
Article
Keywords

CYCLIC GMP-AMP; INNATE IMMUNE SENSOR; SYNTHASE; 2ND-MESSENGER; DINUCLEOTIDE

Citation

FEBS LETTERS, v.591, no.6, pp.954 - 961

ISSN
1873-3468
DOI
10.1002/1873-3468.12598
URI
http://hdl.handle.net/10203/223512
Appears in Collection
CH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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