Autoacetylation of NAT10 is critical for its function in rRNA transcription activation.

Shiying Cai, Xiaofeng Liu, Chunfeng Zhang, Baocai Xing, Xiaojuan Du

Biochemical and biophysical research communications 2017 Jan 29

filter terms:

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. Copyright © 2016 Elsevier Inc. All rights reserved.

Citation

Shiying Cai, Xiaofeng Liu, Chunfeng Zhang, Baocai Xing, Xiaojuan Du. Autoacetylation of NAT10 is critical for its function in rRNA transcription activation. Biochemical and biophysical research communications. 2017 Jan 29;483(1):624-629