Expression of the Escherichia coli IrgA homolog adhesin is regulated by the ferric uptake regulation protein.

Rashid, RA; Tarr, PI; Moseley, SL

Expression of the Escherichia coli IrgA homolog adhesin is regulated by the ferric uptake regulation protein.

Rashid, RA Tarr, PI Moseley, SL

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Publication Type:: Journal Article
Citation:: Microb Pathog, 2006, 41 (6), pp. 207 - 217
Issue Date:: 2006-12

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Field	Value	Language
dc.contributor.author	Rashid, RA	en_US
dc.contributor.author	Tarr, PI	en_US
dc.contributor.author	Moseley, SL	en_US
dc.date.available	2006-07-27	en_US
dc.date.issued	2006-12	en_US
dc.identifier.citation	Microb Pathog, 2006, 41 (6), pp. 207 - 217	en_US
dc.identifier.issn	0882-4010	en_US
dc.identifier.uri	http://hdl.handle.net/10453/3724
dc.description.abstract	The IrgA homolog adhesin (Iha) is an adherence-conferring outer membrane protein of Escherichia coli associated with enterohemorrhagic and uropathogenic strains. Here, we used primer extension analysis to identify iha promoters in O157:H7 and uropathogenic E. coli strains. Transcriptional fusions demonstrated that iha transcription is repressed by iron. Gel shifts using purified ferric uptake regulator protein (Fur) demonstrated that repression involves a direct interaction between Fur and the iha promoter. We identified strain-dependent differences in iha expression and determined that single nucleotide polymorphisms upstream of the iha promoter, in particular position -85, contribute to differences in expression levels.	en_US
dc.language	eng	en_US
dc.relation.ispartof	Microb Pathog	en_US
dc.relation.isbasedon	10.1016/j.micpath.2006.07.006	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Escherichia coli O157	en_US
dc.subject.mesh	Ferric Compounds	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Adhesins, Escherichia coli	en_US
dc.subject.mesh	Repressor Proteins	en_US
dc.subject.mesh	RNA, Bacterial	en_US
dc.subject.mesh	Bacterial Adhesion	en_US
dc.subject.mesh	Transcription, Genetic	en_US
dc.subject.mesh	Gene Expression Regulation, Bacterial	en_US
dc.subject.mesh	Base Sequence	en_US
dc.subject.mesh	Polymorphism, Single Nucleotide	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Promoter Regions, Genetic	en_US
dc.subject.mesh	Single-Strand Specific DNA and RNA Endonucleases	en_US
dc.title	Expression of the Escherichia coli IrgA homolog adhesin is regulated by the ferric uptake regulation protein.	en_US
dc.type	Journal Article
utslib.citation.volume	6	en_US
utslib.citation.volume	41	en_US
utslib.location.activity	England	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	1107 Immunology	en_US
utslib.for	1108 Medical Microbiology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
utslib.copyright.status	closed_access
pubs.issue	6	en_US
pubs.publication-status	Published	en_US
pubs.volume	41	en_US

Abstract:

The IrgA homolog adhesin (Iha) is an adherence-conferring outer membrane protein of Escherichia coli associated with enterohemorrhagic and uropathogenic strains. Here, we used primer extension analysis to identify iha promoters in O157:H7 and uropathogenic E. coli strains. Transcriptional fusions demonstrated that iha transcription is repressed by iron. Gel shifts using purified ferric uptake regulator protein (Fur) demonstrated that repression involves a direct interaction between Fur and the iha promoter. We identified strain-dependent differences in iha expression and determined that single nucleotide polymorphisms upstream of the iha promoter, in particular position -85, contribute to differences in expression levels.

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http://hdl.handle.net/10453/3724