TY - JOUR
T1 - Methionine Adenosyltransferase II Serves as a Transcriptional Corepressor of Maf Oncoprotein
AU - Katoh, Yasutake
AU - Ikura, Tsuyoshi
AU - Hoshikawa, Yutaka
AU - Tashiro, Satoshi
AU - Ito, Takashi
AU - Ohta, Mineto
AU - Kera, Yohei
AU - Noda, Tetsuo
AU - Igarashi, Kazuhiko
N1 - Funding Information:
We thank Dr. H. Motohashi (Tohoku University) for critical reading of the manuscript and comments; C. Teruya (Tohoku University) for mass spectrometric analysis; Drs. K. Itoh, A. Maruyama (Hirosaki University), J. Sharif, Y. Dohi, A. Muto, K. Murayama (Tohoku University), and M. Matsumoto and K. Nakayama (Kyusyu University) for discussion and help; Dr. H. Kimura (Osaka University) for antibodies to methylated H3K4 and H3K9, and acetylated H3K9 and H3K27; and Dr. M. Tachibana (Kyoto University) for HMT assay protocol. The biotin tag system was kindly provided by Dr. A.B. Cantor (Children's Hospital Boston). This work was supported by Grants-in-aid from the Ministry of Education, Science, Sport, and Culture of Japan, grant from the Naito Foundation for Research on “Nuclear Dynamics and RNA,” grant from the Nukada scholarship, Toho University, and global COE program for Network Medicine, Tohoku University. Part of this study was supported by Biomedical Research Core of Tohoku University School of Medicine.
PY - 2011/3/4
Y1 - 2011/3/4
N2 - Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. However, the function of MAT in the nucleus is largely unknown. MafK represses or activates expression of heme oxygenase-1 (HO-1) gene, depending on its heterodimer partners. Proteomics analysis of MafK revealed its interaction with MATIIα, a MAT isozyme. MATIIα was localized in nuclei and found to form a dense network with chromatin-related proteins including Swi/Snf and NuRD complexes. MATIIα was recruited to Maf recognition element (MARE) at HO-1 gene. When MATIIα was knocked down in murine hepatoma cell line, expression of HO-1 was derepressed at both basal and induced levels. The catalytic activity of MATIIα, as well as its interacting factors such as MATIIβ, BAF53a, CHD4, and PARP1, was required for HO-1 repression. MATII serves as a transcriptional corepressor of MafK by interacting with chromatin regulators and supplying SAM for methyltransferases.
AB - Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. However, the function of MAT in the nucleus is largely unknown. MafK represses or activates expression of heme oxygenase-1 (HO-1) gene, depending on its heterodimer partners. Proteomics analysis of MafK revealed its interaction with MATIIα, a MAT isozyme. MATIIα was localized in nuclei and found to form a dense network with chromatin-related proteins including Swi/Snf and NuRD complexes. MATIIα was recruited to Maf recognition element (MARE) at HO-1 gene. When MATIIα was knocked down in murine hepatoma cell line, expression of HO-1 was derepressed at both basal and induced levels. The catalytic activity of MATIIα, as well as its interacting factors such as MATIIβ, BAF53a, CHD4, and PARP1, was required for HO-1 repression. MATII serves as a transcriptional corepressor of MafK by interacting with chromatin regulators and supplying SAM for methyltransferases.
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U2 - 10.1016/j.molcel.2011.02.018
DO - 10.1016/j.molcel.2011.02.018
M3 - Article
C2 - 21362551
AN - SCOPUS:79951974172
VL - 41
SP - 554
EP - 566
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 5
ER -