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

Authors :
Françoise Paquet
Marie-Josèphe Giraud-Panis
Hervé Meudal
Gérard Lancelot
Yann Bilbille
Centre de biophysique moléculaire (CBM)
Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)
Source :
Comptes Rendus. Chimie, Comptes Rendus. Chimie, Académie des sciences (Paris), 2006, 9 (3-4), pp.452-458. ⟨10.1016/j.crci.2005.06.019⟩
Publication Year :
2006
Publisher :
HAL CCSD, 2006.

Abstract

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.

Details

Language :
English
ISSN :
16310748 and 18781543
Database :
OpenAIRE
Journal :
Comptes Rendus. Chimie, Comptes Rendus. Chimie, Académie des sciences (Paris), 2006, 9 (3-4), pp.452-458. ⟨10.1016/j.crci.2005.06.019⟩
Accession number :
edsair.doi.dedup.....111ba85e473bfad2c7f258931473c3fa
Full Text :
https://doi.org/10.1016/j.crci.2005.06.019⟩