Mono-ADP-ribosylation of histone 3 at arginine-117 promotes proliferation through its interaction with P300

Feng Ling, Yi Tang, Ming Li, Qing-Shu Li, Xian Li, Lian Yang, Wei Zhao, Cong-Cong Jin, Zhen Zeng, Chang Liu, Cheng-Fang Wu, Wen-Wen Chen, Xiao Lin, Ya-Lan Wang, Michael Threadgill

Research output: Contribution to journalArticlepeer-review

41 Downloads (Pure)

Abstract

Relatively little attention has been paid to ADP-ribosylated modifications of histones, especially to mono-ADP-ribosylation. As an increasing number of mono-ADP-ribosyltransferases have been identified in recent studies, the functions of mono-ADP-ribosylated proteins have aroused research interest. In particular, histones are substrates of some mono-ADP-ribosyltransferases and mono-ADP-ribosylated histone have been detected in physiological or pathological processes. In this research , arginine-117 (Arg-117; R-117) of histone3(H3) is identified as a site of mono-ADP-ribosylation in colon carcinoma(the first such site to be identified); this posttranslational modification may promote the proliferation of colon carcinoma cells in vitro and in vivo. Using a point-mutant lentivirus transfection and using an activator of P300 allowed us to observe the mono-ADP-ribosylation at H3R117 and enhancement of the activity of P300 to up-regulate the level of acetylated β-catenin, which could increase the expression of c-myc and cyclin D1.
Original languageEnglish
Pages (from-to)72773-72787
Number of pages15
JournalOncotarget
Volume8
Issue number42
DOIs
Publication statusPublished - 18 Aug 2017

Fingerprint Dive into the research topics of 'Mono-ADP-ribosylation of histone 3 at arginine-117 promotes proliferation through its interaction with P300'. Together they form a unique fingerprint.

Cite this