Reference : Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transac...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/32296
Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transactivation of the matrix metalloproteinase-13 gene.
English
Samuel, Shaija [> > > >]
Twizere, Jean-Claude mailto [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
Beifuss, Katherine K [> > > >]
Bernstein, Lori R [> > > >]
2008
Molecular Carcinogenesis
Wiley Liss, Inc.
47
1
34-46
Yes (verified by ORBi)
International
0899-1987
1098-2744
New York
NY
[en] Adenocarcinoma ; Amino Acid Sequence ; Base Sequence ; Cell Line, Tumor ; DNA/chemistry/genetics/metabolism ; Humans ; Mass Spectrometry ; Matrix Metalloproteinase 13/genetics ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Phosphoproteins/metabolism ; Plasmids ; Protein Binding ; RNA-Binding Proteins/metabolism ; Transcription Factor AP-1/genetics/metabolism ; Transcriptional Activation
[en] Transcriptional regulation via activator protein-1 (AP-1) protein binding to AP-1 binding sites within gene promoter regions of AP-1 target genes plays a key role in controlling cellular invasion, proliferation, and oncogenesis, and is important to pathogenesis of arthritis and cardiovascular disease. To identify new proteins that interact with the AP-1 DNA binding site, we performed the DNA affinity chromatography-based Nucleotide Affinity Preincubation Specificity TEst of Recognition (NAPSTER) assay, and discovered a 97 kDa protein that binds in vitro to a minimal AP-1 DNA sequence element. Mass spectrometric fragmentation sequencing determined that p97 is nucleolin. Immunoblotting of DNA affinity-purified material with anti-nucleolin antibodies confirmed this identification. Nucleolin also binds the AP-1 site in gel shift assays. Nucleolin interacts in NAPSTER with the AP-1 site within the promoter sequence of the metalloproteinase-13 gene (MMP-13), and binds in vivo in chromatin immunoprecipitation assays in the vicinity of the AP-1 site in the MMP-13 promoter. Overexpression of nucleolin in human HeLa cervical carcinoma cells significantly represses AP-1 dependent gene transactivation of a minimal AP-1 reporter construct and of an MMP-13 promoter reporter sequence. This is the first report of nucleolin binding and transregulation at the AP-1 site.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/32296
10.1002/mc.20358
(c) 2007 Wiley-Liss, Inc.

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