Interaction of human Ku70 with TRF2

Ku, a heterodimer of 70- and 80-kDa subunits, plays a general role in the metabolism of DNA ends in eukaryotic cells, including double-strand DNA break repair, V(D)J recombination, and maintenance of telomeres. We have utilized the yeast two-hybrid system to identify Ku70-interacting proteins other...

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Veröffentlicht in:	FEBS letters 2000-09, Vol.481 (1), p.81-85
Hauptverfasser:	Song, Kyuyoung, Jung, Donghae, Jung, Yusun, Lee, Seong-Gene, Lee, Inchul
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antigens, Nuclear Base Sequence Binding Sites COS Cells Dimerization DNA Helicases DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism DNA-PK, DNA-dependent protein kinase DTT, dithiothreitol FITC, fluorescein isothiocyanate Fluorescent Antibody Technique Humans Ku Autoantigen Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism PMSF, phenylmethylsulfonyl fluoride Precipitin Tests Protein Binding Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Repetitive Sequences, Amino Acid Saccharomyces cerevisiae Proteins Telomere Telomere - genetics Telomere - metabolism Telomeric Repeat Binding Protein 2 Transfection TRF2 Two-Hybrid System Techniques Yeast two-hybrid
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Zusammenfassung:	Ku, a heterodimer of 70- and 80-kDa subunits, plays a general role in the metabolism of DNA ends in eukaryotic cells, including double-strand DNA break repair, V(D)J recombination, and maintenance of telomeres. We have utilized the yeast two-hybrid system to identify Ku70-interacting proteins other than Ku80. Two reactive clones were found to encode the dimerization domain of TRF2, a mammalian telomeric protein that binds to duplex TTAGGG repeats at chromosome ends. This interaction was confirmed using bacterial fusion proteins and co-immunoprecipitations from eukaryotic cells overexpressing TRF2. The transfected TFR2 colocalized with Ku70.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(00)01958-X