Backbone assignment of the three dimers of HU from Escherichia coli at 293 K: EcHUα2, EcHUβ2 and EcHUαβ.
HU is one of the major nucleoid-associated proteins involved in bacterial chromosome structure and in all DNA-dependent cellular activities. Similarly to eukaryotic histones, this small dimeric basic protein wraps DNA in a non-sequence specific manner, promoting DNA super-structures. In most bacteria, HU is a homodimeric protein encoded by a single gene. However, in enterobacteria such as Escherichia coli, the presence of two genes coding for two peptidic chains, HUα and HUβ, lead to the coexistence of three forms: two homodimers EcHUα2 and EcHUβ2, as well as a heterodimer EcHUαβ. Genetic and biochemical investigation suggest that each EcHU dimer plays a specific physiological role in bacteria. Their relative abundance depends on the environmental conditions and is driven by an essential, yet unknown, fast outstanding chain-exchange mechanism at physiological temperature. Our goal is to understand this fundamental mechanism from a structural and kinetics standpoint using NMR. For this purpose, the first steps are the assignment of each dimer in their native and intermediate states. Here, we report the backbone assignment of each HU dimers from E. coli at 293 K in their native state.
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
Rémy
R
Le Meur
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France. karine.loth@cnrs-orleans.fr.
Karine
K
Loth
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
Françoise
F
Culard
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
Bertrand
B
Castaing
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
Céline
C
Landon
D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D016415:Sequence Alignment
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C116822:hns protein, E coli
Dimers; E. coli; HU; Histone-like