Accueil > Publications > Recherche par années > Années 2010 > 2011

Garnier, N., Loth, K., Coste, F. Augustyniak, R., Nadan, V., Damblon, C. & Castaing, B..

An alternative flexible conformation of the E. coli HUβ(2) protein : structural, dynamics, and functional aspects.

European Biophysics Journal 40 (2) 117-129

par Administrateur - publié le , mis à jour le

Abstract :

The histone-like HU protein is the major nucleoid-associated protein involved in the dynamics and structure of the bacterial chromosome. Under physiological conditions, the three possible dimeric forms of the E. coli HU protein (EcHUα₂, EcHUβ₂, and EcHUαβ) are in thermal equilibrium between two dimeric conformations (N₂ ↔ I₂) varying in their secondary structure content. High-temperature molecular dynamics simulations combined with NMR experiments provide information about structural and dynamics features at the atomic level for the N₂ to I₂ thermal transition of the EcHUβ₂ homodimer. On the basis of these data, a realistic 3D model is proposed for the major I₂ conformation of EcHUβ₂. This model is in agreement with previous experimental data.