TY - JOUR
T1 - EHMT1 protein binds to nuclear factor-κB p50 and represses gene expression
AU - Ea, Chee Kwee
AU - Hao, Sheng Li
AU - Yeo, Kok Siong
AU - Baltimore, David
PY - 2012/9/7
Y1 - 2012/9/7
N2 - Transcriptional homeostasis relies on the balance between positive and negative regulation of gene transcription. Methylation of histone H3 lysine 9 (H3K9) is commonly correlated with gene repression. Here, we report that a euchromatic H3K9 methyltransferase, EHMT1, functions as a negative regulator in both the NF-κB- and type I interferon-mediated gene induction pathways. EHMT1 catalyzes H3K9 methylation at promoters of NF-κB target genes. Moreover, EHMT1 interacts with p50, and, surprisingly, p50 appears to repress the expression of type I interferon genes and genes activated by type I interferons by recruiting EHMT1 to catalyze H3K9 methylation at their promoter regions. Silencing the expression of EHMT1 by RNA interference enhances expression of a subset NF-κB-regulated genes, augments interferon production, and augments antiviral immunity.
AB - Transcriptional homeostasis relies on the balance between positive and negative regulation of gene transcription. Methylation of histone H3 lysine 9 (H3K9) is commonly correlated with gene repression. Here, we report that a euchromatic H3K9 methyltransferase, EHMT1, functions as a negative regulator in both the NF-κB- and type I interferon-mediated gene induction pathways. EHMT1 catalyzes H3K9 methylation at promoters of NF-κB target genes. Moreover, EHMT1 interacts with p50, and, surprisingly, p50 appears to repress the expression of type I interferon genes and genes activated by type I interferons by recruiting EHMT1 to catalyze H3K9 methylation at their promoter regions. Silencing the expression of EHMT1 by RNA interference enhances expression of a subset NF-κB-regulated genes, augments interferon production, and augments antiviral immunity.
UR - http://www.scopus.com/inward/record.url?scp=84866127152&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84866127152&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.365601
DO - 10.1074/jbc.M112.365601
M3 - Article
C2 - 22801426
AN - SCOPUS:84866127152
SN - 0021-9258
VL - 287
SP - 31207
EP - 31217
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 37
ER -