@article{10272/7491,
year = {2002},
month = {9},
url = {http://hdl.handle.net/10272/7491},
abstract = {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.},
publisher = {American Society for Microbiology},
title = {Temperature- and H-NS-Dependent Regulation of a Plasmid-Encoded Virulence Operon Expressing Escherichia coli Hemolysin},
doi = {10.1128/JB.184.18.5058–5066.2002},
author = {Madrid, Cristina and Nieto Liñán, José Miguel and Paytubi, Sònia and Falconi, Maurizio and Gualerzi, Claudio O. and Juárez, Antonio},
}