Temperature- and H-NS-Dependent Regulation of a Plasmid-Encoded Virulence Operon Expressing Escherichia coli Hemolysin

Proteins H-NS and Hha form a nucleoprotein complex that modulates expression of the thermoregulated hly operon of Escherichia coli. We have been able to identify two H-NS binding sites in the hly regulatory region. One of them partially overlaps the promoter region (site II), and the other is locate...

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Bibliographic Details
Authors: Madrid, Cristina, Nieto Liñán, José Miguel, Paytubi, Sònia, Falconi, Maurizio, Gualerzi, Claudio O., Juárez, Antonio
Format: article
Publication Date:2002
Country:España
Institution:Universidad de Huelva (UHU)
Repository:Arias Montano. Repositorio Institucional de la Universidad de Huelva
Language:English
OAI Identifier:oai:ariasmontano.uhu.es:10272/7491
Online Access:http://hdl.handle.net/10272/7491
Access Level:Open access
Keyword:H-NS
Hha
Escherichia coli
Description
Summary:Proteins H-NS and Hha form a nucleoprotein complex that modulates expression of the thermoregulated hly operon of Escherichia coli. We have been able to identify two H-NS binding sites in the hly regulatory region. One of them partially overlaps the promoter region (site II), and the other is located about 2 kbp upstream (site I). In contrast, Hha protein did not show any preference for specific sequences. In vitro, temperature influences the affinity of H-NS for a DNA fragment containing both binding sites and H-NS-mediated repression of hly operon transcription. Deletion analysis of the hly regulatory region confirms the relevance of site I for thermoregulation of this operon. We present a model to explain the temperature-modulated repression of the hly operon, based on the experiments reported here and other, preexisting data.