Multiple co-regulatory elements and IHF are necessary for the control of fimB expression in response to sialic acid and N-acetylglucosamine in Escherichia coli K-12

Sohanpal, B.K. and Friar, S. and Roobol, J. and Plumbridge, J.A. and Blomfield, I.C. (2007) Multiple co-regulatory elements and IHF are necessary for the control of fimB expression in response to sialic acid and N-acetylglucosamine in Escherichia coli K-12. Molecular Microbiology, 63 (4). pp. 1223-1236. ISSN 0950-382X. (The full text of this publication is not available from this repository)

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Abstract

Expression of the FimB recombinase, and hence the OFF-to-ON switching of type 1 fimbriation in Escherichia coli, is inhibited by sialic acid (Neu(5)Ac) and by GlcNAc. NanR (Neu(5)Ac-responsive) and NagC (GlcNAc-6P-responsive) activate fimB expression by binding to operators (O-NR and O-NC1 respectively) located more than 600 bp upstream of the fimB promoter within the large (1.4 kb) nanC-fimB intergenic region. Here it is demonstrated that NagC binding to a second site (O-NC2), located 212 bp closer to fimB, also controls fimB expression, and that integration host factor (IHF), which binds midway between O-NC1 and O-NC2, facilitates NagC binding to its two operator sites. In contrast, IHF does not enhance the ability of NanR to activate fimB expression in the wild-type background. Neither sequences up to 820 bp upstream of O-NR, nor those 270 bp downstream of O-NC2, are required for activation by NanR and NagC. However, placing the NanR, IHF and NagC binding sites closer to the fimB promoter enhances the ability of the regulators to activate fimB expression. These results support a refined model for how two potentially key indicators of host inflammation, Neu(5)Ac and GlcNAc, regulate type 1 fimbriation.

Item Type: Article
Uncontrolled keywords:
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Jane Griffiths
Date Deposited: 19 Dec 2007 17:43
Last Modified: 14 Jan 2010 14:05
Resource URI: http://kar.kent.ac.uk/id/eprint/2184 (The current URI for this page, for reference purposes)
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