Neural Regeneration Research ›› 2021, Vol. 16 ›› Issue (7): 1427-1428.doi: 10.4103/1673-5374.301006

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Role of N4-acetylcytidine for continuously activating NLRP3 inflammosome by HMGB1 pathway in microglia  

Hua Bai*, Qifang Zhang   

  1. Department of Neurology, Medical Experimental Center, the Third Affiliated Hospital of Guizhou Medical University, Duyun; Department of Neurology, Affiliated Hospital of Guizhou Medical  University, Guiyang, Guizhou Province, China 
    (Bai H)
    Key Laboratory of Endemic and Ethnic Diseases, Ministry of Education, Key Laboratory of Medical Molecular Biology, Guizhou Medical University, Guiyang, Guizhou Province, China (Zhang Q)
  • Online:2021-07-15 Published:2021-01-07
  • Contact: Hua Bai, MD, PhD, baih2020@gmc.edu.cn.
  • Supported by:
    This work was supported by the grant from Guizhou Science and Technology Department Support Plan Project in China, No. Qiankehe-zhicheng [2020]4Y129 (to HB).

Abstract: N4-acetylcytidine (N4A) is an organic compound and a metabolite of transferrable ribonucleic acid. Its molecular formula is C11H15N3O6. Preliminary studies suggest that N4A was mainly found on tRNA and 18S rRNA, while recent studies have shown that there is also a large amount of N4A on mRNA, whose abundance is not even lower than the m7G cap modification carried by mRNA (Arango et al., 2018). The generation of N4A is catalyzed by N-acetyltransferase 10 (NAT10) or its homologous enzyme. N4A is produced by acetylation in eukaryotic RNA and is the only human enzyme with both acetyltransferase and RNA binding activity (Arango et al., 2018). The full transcriptome mapping of N4A shows abundant discrete acetylation regions in the coding sequence. The ablation of NAT10 reduces the detection of N4A at mRNA localization sites and is globally correlated with the down-regulation of tmRNA. N4A is widely distributed in the human transcriptome, and most sites occur in the coding sequence. Compared with unmodified cytosine, N4A increases the thermal stability of Watson-Crick base pair guanosine, thus affecting the interaction with homologous tRNAs during translation. After the release of N4A from tRNA metabolism, it participates in the systematic immune response (Ito et al., 2014).