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Suv39H1 Recruitment by Sp1 Causes a Decline in 12(S)‐Lipoxygenase Expression
Author(s) -
Chuang JianYing,
Chang WenChang,
Hung JanJong
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.678.6
Subject(s) - histone methyltransferase , methylation , sumo protein , biology , demethylase , microbiology and biotechnology , dna methylation , histone methylation , sp1 transcription factor , histone , chemistry , gene expression , gene , genetics , promoter , ubiquitin
Sp1 is an important transcription factor that regulates gene expression. Several modifications such as phosphorylation, acetylation, glycosylation, ubiquitination, and sumoylation have been found in Sp1, and these affect its transcriptional activity. In this study, we found that Sp1 can directly interact with the methyltransferase Suv39H1 and that it is also modified by methylation. In addition, to inhibit the lynsine‐specific demethylase 1 with pargyline or Suv39H1 overexpression would increase the Sp1 methylation signal. In the early stages of mitosis, the Suv39H1 protein level increases and co‐localizes with Sp1. Sp1 plays the role of an anchor protein, recruiting Suv39H1 to the chromatin region in order to methylate histone H3, which leads to chromosome packaging during mitosis. In addition, the increase in Sp1 methylation represses the expression of Sp1 target gene, 12(S)‐Lipoxygenase. Taken together, these data indicate that Suv39H1 could be recruited to the genomic region by Sp1 to affect the Sp1‐denpendent gene expression through modulation of the post‐translational modification of Sp1 and histone H3 by methylation.