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Dynamic Cycling of the O‐GlcNAc Transferase on the Estrogen Responsive pS2 Promoter During the Transcription Cycle.
Author(s) -
Sakabe Kaoru,
Hart Gerald W.
Publication year - 2007
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.21.5.a286
Subject(s) - serine , threonine , phosphorylation , transcription (linguistics) , coactivator , biochemistry , transcription factor , transferase , promoter , transcriptional regulation , biology , kinase , chemistry , enzyme , microbiology and biotechnology , gene expression , gene , linguistics , philosophy
Enzymatic modification of serine and threonine residues on nucleocytoplasmic proteins with a single N‐acetylglucosamine moiety through a ?‐glycosidic linkage (O‐GlcNAc) is a dynamic post‐translational modification. Much like phosphorylation, protein O‐GlcNAcylation is responsive to cell stimuli and can serve to regulate protein function. However, while there are a large number of different kinases and phosphatases, only a single O‐GlcNAc Transferase (OGT) and O‐GlcNAcase have been identified in mammals. Recently, through a yeast two‐hybrid approach, we have identified Coactivator Associated Arginine Methyltransferase (CARM1) as a putative binding partner with OGT. CARM1 has been shown by other groups to methylate Arg residues of proteins such as p300 and histone H3. Additionally, CARM1 is required for maximal transcriptional activation of nuclear hormone receptor mediated transcription. Furthermore, CARM1, as well as other components of the transcriptional machinery, associates cyclically with the estrogen responsive pS2 promoter. We have recently shown that not only does CARM1 bind OGT, but also it itself is an O‐GlcNAc modified protein. Our data indicate that the O‐GlcNAc processing enzymes also cycle on and off the pS2 promoter and are involved in the transcription regulation at the pS2 promoter. Supported by NIH grant CA42486. Dr. Hart receives a share of royalty received by the university on sales of the CTD110.6 antibody. Terms of this arrangement are managed by JHU.