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Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transactivation of the matrix metalloproteinase-13 gene by Shaija Samuel; Jean-Claude Twizere; Katherine K. Beifuss; Lori R. Bernstein is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract 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

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Author

Shaija Samuel; Jean-Claude Twizere; Katherine K. Beifuss; Lori R. Bernstein

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0899-1987)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)