Literature DB >> 16030239

Functional replacement of the oligomerization domain of H-NS by the Hha protein of Escherichia coli.

Sonia Rodríguez1, José María Nieto, Cristina Madrid, Antonio Juárez.   

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.

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Year:  2005        PMID: 16030239      PMCID: PMC1196020          DOI: 10.1128/JB.187.15.5452-5459.2005

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  41 in total

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Authors:  M Mouriño; F Muñoa; C Balsalobre; P Diaz; C Madrid; A Juarez
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9.  ymoA, a Yersinia enterocolitica chromosomal gene modulating the expression of virulence functions.

Authors:  G R Cornelis; C Sluiters; I Delor; D Geib; K Kaniga; C Lambert de Rouvroit; M P Sory; J C Vanooteghem; T Michiels
Journal:  Mol Microbiol       Date:  1991-05       Impact factor: 3.501

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3.  Controlling biofilm formation, prophage excision and cell death by rewiring global regulator H-NS of Escherichia coli.

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