Abstract
Sp1 is a ubiquitous transcription factor that is modified by multiple O-linked N-acetylglucosamines (O-GlcNAc). Previously, O-GlcNAcylation of a specific site of Sp1 was shown to inhibit Sp1 transcriptional activity. Yet, how O-GlcNAc on other modification sites affects Sp1 function and how O-GlcNAcylation of Sp1 affects the transcriptional regulation of a target gene remains unknown. Here we show that O-GlcNAc within the second serine/threonine-rich region of Sp1 interrupts a known interaction between Sp1 and Oct1, and inhibits the cooperative activation of the U2 snRNA gene by Sp1 and Oct1. Structured summary: MINT-6803452: Sp1 (uniprotkb-P08047) physically interacts (MI:0218) with Oct1 (uniprotkb:P14859) by anti tag coimmunoprecipitation (MI:0007). MINT-6803426, MINT-6803438: Oct1 (uniprotkb:P14859) binds (MI:0407) to Sp1 (uniprotkb:P08047) by pull down (MI:0096). MINT-6803470, MINT-6803484: Sp1 (uniprotkb:P08047) physically interacts (MI:0218) with Oct1 (uniprotkb:P14859) by anti bait coimmunoprecipitation (MI:0006).
Original language | English |
---|---|
Pages (from-to) | 512-520 |
Number of pages | 9 |
Journal | FEBS Letters |
Volume | 583 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2009 Feb 4 |
Keywords
- O-GlcNAc
- Oct1
- Sp1
- U2 snRNA
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology