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

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

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 (EcHU alpha(2), EcHU beta(2), and EcHU alpha beta) are in thermal equili...

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Bibliographic Details
Published in:European biophysics journal Vol. 40; no. 2; pp. 117 - 129
Main Authors: Garnier, Norbert, Loth, Karine, Coste, Franck, Augustyniak, Rafal, Nadan, Virginie, Damblon, Christian, Castaing, Bertrand
Format: Journal Article
Language:English
Published: Springer Verlag (Germany) 01-02-2011
Subjects:
Life Sciences
HISTONE-LIKE PROTEIN
SPECTROSCOPY
HU PROTEIN
ESCHERICHIA-COLI
CHEMICAL-SHIFT
THERMOSTABILITY
BACILLUS-STEAROTHERMOPHILUS
DNA-BINDING PROTEIN
THERMOTOGA-MARITIMA
BETA
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Summary: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 (EcHU alpha(2), EcHU beta(2), and EcHU alpha beta) are in thermal equilibrium between two dimeric conformations (N-2 a dagger" I-2) 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 N-2 to I-2 thermal transition of the EcHU beta(2) homodimer. On the basis of these data, a realistic 3D model is proposed for the major I-2 conformation of EcHU beta(2). This model is in agreement with previous experimental data.
ISSN:0175-7571
1432-1017
DOI:10.1007/s00249-010-0630-y