NMR studies of telomeric nucleoprotein complexes involving the Myb-like domain of the human telomeric protein TRF2

Y. Bilbille (1) , F. Paquet (1) , H. Meudal (1) , M.J. Giraud-Panis (1) , G. Lancelot (1)

1 CBM - Centre de biophysique moléculaire

In order to study the binding of the Myb-like domain of the human telomeric protein TRF2 (Myb-TRF2) with different structural components of the t-loop model, we report NMR studies of the binding of Myb-TRF2 protein with two repeats human telomeric DNA under three conformations. Our results showed that Myb-TRF2 binds to the duplex and even to the quadruplex and the random coil G-rich strand. The solution structure of Myb-TRF2 reported here looks like Myb-TRF1 suggesting similar DNA binding mode. As a matter of fact, we have shown that its binding to the human telomeric duplex presents great similarities with this of Myb-TRF1.

Mots clés: Molecular complex; DNA; Molecular interaction; Human; Transcription factor; Protooncogene; Nucleoprotein; Telomere; NMR spectrometry

Y. Bilbille, F. Paquet, H. Meudal, M.J. Giraud-Panis, G. Lancelot. NMR studies of telomeric nucleoprotein complexes involving the Myb-like domain of the human telomeric protein TRF2. Comptes Rendus. Chimie, 2006, 9 (3-4), pp.452-458. ⟨10.1016/j.crci.2005.06.019⟩. ⟨hal-00088835⟩