PMID:16030239

Citation	Rodríguez, S, Nieto, JM, Madrid, C and Juárez, A (2005) Functional replacement of the oligomerization domain of H-NS by the Hha protein of Escherichia coli. J. Bacteriol. 187:5452-9
Abstract	Members of the H-NS family of proteins play a relevant role as modulators of gene expression in gram-negative bacteria. Interaction of these proteins with members of the Hha/YmoA family of proteins has been previously reported. It has been hypothesized that the latter proteins are functionally equivalent to the N-terminal domain of H-NS-like proteins. In this report we test this assumption by replacing the N-terminal domain of Escherichia coli H-NS by Hha. It has been possible to obtain a functional protein that can compensate for some of the hns-induced phenotypes. These results highlight the relevance of H-NS-Hha interactions to generate heterooligomeric complexes that modulate gene expression in gram-negative bacteria.
Links	PubMed PMC1196020 Online version:10.1128/JB.187.15.5452-5459.2005
Keywords	Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; DNA-Binding Proteins/physiology; Dimerization; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Molecular Sequence Data; Oligopeptides/metabolism; Protein Structure, Tertiary; Recombination, Genetic
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