In Vitro Binding of Nucleolin to Double-Stranded Telomeric DNA

We have purified a 100 kDa protein, resolved in a Southwestern binding screen of total nuclear proteins from Hela cells with double-stranded human telomeric probe. A polyclonal antiserum raised by this protein recognizes purified nucleolin and stains nucleoli in growing Hela cells. We demonstrate th...

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Veröffentlicht in:	Biochemical and biophysical research communications 2000-02, Vol.268 (3), p.909-915
Hauptverfasser:	Pollice, Alessandra, Zibella, Maria Pia, Bilaud, Thomas, Laroche, Thierry, Pulitzer, John F., Gilson, Eric
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies Base Sequence Binding Sites - genetics Cell Nucleolus - metabolism DNA - genetics DNA - metabolism DNA-binding Escherichia coli - genetics HeLa Cells Humans In Vitro Techniques Life Sciences mammalian Mice Nuclear Proteins - genetics Nuclear Proteins - metabolism Nucleolin Phosphoproteins - genetics Phosphoproteins - metabolism Protein Binding Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism telomere Telomere - metabolism
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Beschreibung
Zusammenfassung:	We have purified a 100 kDa protein, resolved in a Southwestern binding screen of total nuclear proteins from Hela cells with double-stranded human telomeric probe. A polyclonal antiserum raised by this protein recognizes purified nucleolin and stains nucleoli in growing Hela cells. We demonstrate that a truncated form of human nucleolin and a purified deletion derivative of mouse nucleolin bind in vitro to duplex telomeric DNA. This study suggests a new link between telomeres and the nucleolus.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.2000.2237