Journal
ONCOTARGET
Volume 8, Issue 42, Pages 72773-72787Publisher
IMPACT JOURNALS LLC
DOI: 10.18632/oncotarget.20347
Keywords
site of mono-ADP-ribosylation; histone modification; colon carcinoma; proliferation; P300
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Funding
- Innovation Project of Graduate Student in Chongqing [CYS15140]
- Nursery Plan of Basic Medical College in Chongqing Medical University [40010200010039]
- Scientific Research Foundation of Chongqing Medical University [201413]
- National Nature Science Foundation of China [30870946]
- Science and Technology Plan Project of Yuzhong District in Chongqing [20140106]
- National High Technology Research and Development Program of China [2012AA02A201]
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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 monoADP- 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 hsitone3(H3) is identified as the 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 beta-catenin, which could increase the expression of c-myc and cyclin D1.
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