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

doi:10.18632/oncotarget.20347

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

Department of Life Sciences

Chongqing Medical University

Research output: Contribution to journal › Article › peer-review

12 Citations (SciVal)

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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 language	English
Pages (from-to)	72773-72787
Number of pages	15
Journal	Oncotarget
Volume	8
Issue number	42
DOIs	https://doi.org/10.18632/oncotarget.20347
Publication status	Published - 18 Aug 2017

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20347-292080-4-PBFinal published version, 11.5 MBLicence: CC BY

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

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.",

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

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T1 - Mono-ADP-ribosylation of histone 3 at arginine-117 promotes proliferation through its interaction with P300

AU - Ling, Feng

AU - Tang, Yi

AU - Li, Ming

AU - Li, Qing-Shu

AU - Li, Xian

AU - Yang, Lian

AU - Zhao, Wei

AU - Jin, Cong-Cong

AU - Zeng, Zhen

AU - Liu, Chang

AU - Wu, Cheng-Fang

AU - Chen, Wen-Wen

AU - Lin, Xiao

AU - Wang, Ya-Lan

AU - Threadgill, Michael

PY - 2017/8/18

Y1 - 2017/8/18

N2 - 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.

AB - 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.

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DO - 10.18632/oncotarget.20347

M3 - Article

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EP - 72787

JO - Oncotarget

JF - Oncotarget

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ER -

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

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