Reference : YB-1 represses AP1-dependent gene transactivation and interacts with an AP-1 DNA sequence.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
YB-1 represses AP1-dependent gene transactivation and interacts with an AP-1 DNA sequence.
Samuel, Shaija [> > > >]
Twizere, Jean-Claude mailto [Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
Bernstein, Lori R [> > > >]
Biochemical Journal
Portland Press
Pt 3
Yes (verified by ORBi)
United Kingdom
[en] Base Sequence ; Cell Nucleus ; Chromatography, Affinity ; DNA/genetics/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Down-Regulation ; Electrophoretic Mobility Shift Assay ; Genes, Reporter/genetics ; HT29 Cells ; Hela Cells ; Humans ; Matrix Metalloproteinase 12 ; Metalloendopeptidases/genetics ; Mutation/genetics ; Nuclear Proteins ; Protein Subunits ; Protein Transport ; RNA, Messenger/biosynthesis/genetics ; Substrate Specificity ; Transcription Factor AP-1/antagonists & inhibitors/chemistry/metabolism ; Transcriptional Activation/genetics
[en] Involvement of the AP-1 (activator protein-1) transcription factor has been demonstrated previously in the regulation of cell proliferation and cell-cycle progression, in the control of cell migration, invasion and metastasis, and in signal transduction, stress responsiveness, DNA replication and DNA repair. YB-1 (Y-box-binding protein-1) has also been implicated in many of these processes. However, the mechanism by which YB-1 mediates these processes is poorly understood. In the present study, we report that overexpression of a transfected gene encoding YB-1 in human HeLa cervical carcinoma cells significantly represses the transactivation of a minimal AP-1 reporter construct in response to the tumour promoter PMA. YB-1 also represses mRNA expression and PMA-induced promoter transactivation of the endogenous AP-1 target gene encoding matrix metalloproteinase-12 (metalloelastase). YB-1 transrepression of both the minimal and matrix metalloproteinase-12 promoter reporter constructs is dependent on the AP-1 sequence. To identify new nuclear proteins that bind specifically to the AP-1 DNA-binding site, we devised a DNA-affinity-chromatography-based assay termed NAPSTER (nucleotide-affinity preincubation specificity test of recognition) and discovered a 49 kDa protein from human cancer cells that binds in a sequence-specific manner to the AP-1 DNA sequence. By tandem MS fragmentation sequencing analyses we determined that p49 is a YB-1. Immunoblotting of the NAPSTER-purified p49 protein using anti-YB-1 antibodies confirmed YB-1 binding to the AP-1 DNA sequence, as did gel mobility-supershift assays using YB-1 antibodies. This is the first report of YB-1 transrepression and interaction at the AP-1 DNA-binding site.
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