O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.
O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation. Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain. In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription. Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.
Lim
Kihong
K
School of Life Sciences and Biotechnology, Korea University, 5-1 Anam-dong, Seongbuk-gu, Seoul 136-701, Republic of Korea.
Chang
Hyo-Ihl
HI
D000117:Acetylglucosamine / Q000378:metabolism*; D000215:Acylation; D023081:CCAAT-Binding Factor / Q000378:metabolism*; D002460:Cell Line; D006801:Humans; D047468:Immunoprecipitation; D011401:Promoter Regions, Genetic; D017434:Protein Structure, Tertiary; D016329:Sp1 Transcription Factor / Q000378:metabolism*; D014158:Transcription, Genetic; D015533:Transcriptional Activation
D023081:CCAAT-Binding Factor; C492061:NFYA protein, human; D016329:Sp1 Transcription Factor; D000117:Acetylglucosamine