title: Autoacetylation of NAT10 is critical for its function in rRNA transcription activation.
abstract: NAT10, an important member of GNAT family, harbors histone acetyltransferase and participates in many cellular processes such as ribosome production and cell cycle. Here, we report that NAT10 is acetylated in vivo and autoacetylated in vitro. The lysine residue at 426 (K426) is the acetylation site of NAT10. K426R mutant of NAT10 fails to activate rRNA transcription. NAT10 K426R loses its capability of acetylating UBF though it still binds UBF, which fails to recruit PAF53 and RNA polymerase I to rDNA, eventually resulting in inhibition of pre-rRNA transcription. Therefore, acetylation of K426 in NAT10 is required for its function in activating rRNA transcription. These findings identify a new post-translational modification on NAT10 which regulates its function.
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
authors.forename: Shiying
authors.initials: S
authors.lastname: Cai
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
authors.forename: Xiaofeng
authors.initials: X
authors.lastname: Liu
authors.affiliation: Department of Medical Genetics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
authors.forename: Chunfeng
authors.initials: C
authors.lastname: Zhang
authors.affiliation: Hepatopancreatobiliary Surgery Department I, Key Laboratory of Carcinogenesis and Translational Research, Ministry of Education, Peking University School of Oncology, Beijing Cancer Hospital and Institute, No. 52, Fu-Cheng Road, Beijing 100142, China.
authors.forename: Baocai
authors.initials: B
authors.lastname: Xing
authors.affiliation: Department of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China. Electronic address: duxiaojuan100@bjmu.edu.cn.
authors.forename: Xiaojuan
authors.initials: X
authors.lastname: Du
mesh_terms: D000107:Acetylation; D001665:Binding Sites; D045325:HCT116 Cells; D057809:HEK293 Cells; D006367:HeLa Cells; D006801:Humans; D008239:Lysine / Q000737:chemistry; D009154:Mutation; D063213:N-Terminal Acetyltransferase E / Q000378:metabolism*; D063206:N-Terminal Acetyltransferases; D011499:Protein Processing, Post-Translational; D012318:RNA Polymerase I / Q000378:metabolism; D012335:RNA, Ribosomal / Q000378:metabolism*; D014158:Transcription, Genetic; D015533:Transcriptional Activation
chemical_list: D012335:RNA, Ribosomal; D063213:N-Terminal Acetyltransferase E; D063206:N-Terminal Acetyltransferases; C522989:NAT10 protein, human; D012318:RNA Polymerase I; D008239:Lysine
keywords: Acetylation; Autoacetylation; UBF; rRNA transcription