期刊
FEBS LETTERS
卷 591, 期 6, 页码 954-961出版社
WILEY
DOI: 10.1002/1873-3468.12598
关键词
cGAS; innate immune system; oligomerization
资金
- National Research Foundation of Korea [2011-0020322, 2015 R1A2A2A01005688, 2015R1A2A1A15055329, 2012M3A9B4027955]
- National Research Council of Science and Technology [DRC-14-2-KRISS]
- National Research Foundation of Korea [2015R1A2A1A15055329, 2012M3A9B4027955] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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.
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