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Journal of Bacteriology, August 2005, p. 5452-5459, Vol. 187, No. 15
0021-9193/05/$08.00+0     doi:10.1128/JB.187.15.5452-5459.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Functional Replacement of the Oligomerization Domain of H-NS by the Hha Protein of Escherichia coli

Sonia Rodríguez, José María Nieto, Cristina Madrid, and Antonio Juárez*

Departament de Microbiologia, Facultat de Biologia, Universitat de Barcelona, 08028 Barcelona, Spain

Received 15 February 2005/ Accepted 6 May 2005

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.

* Corresponding author. Mailing address: Departament de Microbiologia, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain. Phone: 34 934034624. Fax: 34 934034629. E-mail: ajuarez{at}ub.edu.

Journal of Bacteriology, August 2005, p. 5452-5459, Vol. 187, No. 15
0021-9193/05/$08.00+0     doi:10.1128/JB.187.15.5452-5459.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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