TY - JOUR
T1 - CARM1 is involved in CYP1A1 gene expression as a transcriptional coactivator
AU - Kim, Yun Jeong
AU - Lim, Yongchul
AU - Lee, Eunil
N1 - Funding Information:
Acknowledgements This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (2016R1D1A1A02937060). Also this study was funded by the Korea Ministry of Environment (MOE) as ‘‘The Environmental Health Action Pro- gram (2016001360007)” and “Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2016R1A6A3 A11930602)”.
Publisher Copyright:
© 2017, The Korean Society of Toxicogenomics and Toxicoproteomics and Springer Science+Business Media B.V.
PY - 2017/9/1
Y1 - 2017/9/1
N2 - Protein arginine methyltransferases (PRMTs) have been proposed as a transcriptional coactivators in the induction of CYP1A1. In this study, we investigated the change of AhR and CYP1A1 expression by inhibition of CARM1 (also known as PRMT4) to show the involvement of protein arginine methylation in CYP1A1 gene expression. Also, we tested the hypothesis that CARM1 recruitment to the CYP1A1 promoter and subsequent histone arginine methylation are required for the activation of transcription. We found that treatment of HepG2 cells with silencing RNA targeting CARM1 or an arginine methyltransferase inhibitor (AMI-5) significantly decreased the CYP1A1 gene expression level. Furthermore, treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), which increases histone arginine methylation in histone H3R17, also caused increases in CARM1 and H3R17 signals in chromatin immunoprecipitation assays. These results indicate that CARM1 is recruited to the CYP1A1 promoter region as a coactivator, and histone arginine methylation makes XRE (xenobiotic responsive element) regions more accessible for transcription.
AB - Protein arginine methyltransferases (PRMTs) have been proposed as a transcriptional coactivators in the induction of CYP1A1. In this study, we investigated the change of AhR and CYP1A1 expression by inhibition of CARM1 (also known as PRMT4) to show the involvement of protein arginine methylation in CYP1A1 gene expression. Also, we tested the hypothesis that CARM1 recruitment to the CYP1A1 promoter and subsequent histone arginine methylation are required for the activation of transcription. We found that treatment of HepG2 cells with silencing RNA targeting CARM1 or an arginine methyltransferase inhibitor (AMI-5) significantly decreased the CYP1A1 gene expression level. Furthermore, treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), which increases histone arginine methylation in histone H3R17, also caused increases in CARM1 and H3R17 signals in chromatin immunoprecipitation assays. These results indicate that CARM1 is recruited to the CYP1A1 promoter region as a coactivator, and histone arginine methylation makes XRE (xenobiotic responsive element) regions more accessible for transcription.
KW - AdOx (adenosine dialdehyde)
KW - AhR (Aryl hydrocarbon receptor)
KW - CARM1 (coactivator associated arginine methyltransferase 1)
KW - CYP1A1 (Cytochrome P4501A1)
KW - PRMT4 (Protein arginine methyltransferase 4)
KW - TCDD (2,3,7,8-tetrachlorodibenzo- p-dioxin)
UR - http://www.scopus.com/inward/record.url?scp=85029834286&partnerID=8YFLogxK
U2 - 10.1007/s13273-017-0029-2
DO - 10.1007/s13273-017-0029-2
M3 - Article
AN - SCOPUS:85029834286
VL - 13
SP - 263
EP - 270
JO - Molecular and Cellular Toxicology
JF - Molecular and Cellular Toxicology
SN - 1738-642X
IS - 3
ER -
