Lactylation of NAT10 promotes N⁴-acetylcytidine modification on tRNA^Ser-CGA-1-1 to boost oncogenic DNA virus KSHV reactivation.

ABSTRACT: N⁴-acetylcytidine (ac⁴C), a conserved but recently rediscovered RNA modification on tRNAs, rRNAs and mRNAs, is catalyzed by N-acetyltransferase 10 (NAT10). Lysine acylation is a ubiquitous protein modification that controls protein functions. Our latest study demonstrates a NAT10-dependent ac⁴C modification, which occurs on the polyadenylated nuclear RNA (PAN) encoded by oncogenic DNA virus Kaposi's sarcoma-associated herpesvirus (KSHV), can induce KSHV reactivation from latency and activate inflammasome. However, it remains unclear whether a novel lysine acylation occurs in NAT10 during KSHV reactivation and how this acylation of NAT10 regulates tRNAs ac⁴C modification. Here, we showed that NAT10 was lactylated by α-tubulin acetyltransferase 1 (

SUBMITTER: Yan Q 

PROVIDER: S-EPMC11445560 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature