Article (Scientific journals)
Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transactivation of the matrix metalloproteinase-13 gene.
Samuel, Shaija; Twizere, Jean-Claude; Beifuss, Katherine K et al.
2008In Molecular Carcinogenesis, 47 (1), p. 34-46
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Keywords :
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
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Samuel, Shaija
Twizere, Jean-Claude  ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Beifuss, Katherine K
Bernstein, Lori R
Language :
Title :
Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transactivation of the matrix metalloproteinase-13 gene.
Publication date :
Journal title :
Molecular Carcinogenesis
Publisher :
Wiley Liss, Inc., New York, United States - New York
Volume :
Issue :
Pages :
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
(c) 2007 Wiley-Liss, Inc.
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