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Genetic and functional characterization of the Escherichia coli BarA-UvrY two-component system: point mutations in the HAMP linker of the BarA sensor give a dominant-negative phenotype
Microbiology and Tumorbiology Center, Karolinska Institutet, SE-171 77 Stockholm, Sweden / Swedish Institute for Infectious Disease Control, SE-17182 Solna, Sweden.
University of Skövde, School of Life Sciences.ORCID iD: 0000-0003-4221-6013
Departamento de Genética Molecular, Instituto de Fisiologia Celular, Universidad National Autónoma de México, 04510 México D.F., Mexico.
Departamento de Genética Molecular, Instituto de Fisiologia Celular, Universidad National Autónoma de México, 04510 México D.F., Mexico.
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2005 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 187, no 21, 7317-7324 p.Article in journal (Refereed) Published
Abstract [en]

The BarA-UvrY two-component system family is strongly associated with virulence but is poorly understood at the molecular level. During our attempts to complement a barA deletion mutant, we consistently generated various mutated BarA proteins. We reasoned that characterization of the mutants would help us to better understand the signal transduction mechanism in tripartite sensors. This was aided by the demonstrated ability to activate the UvrY regulator with acetyl phosphate independently of the BarA sensor. Many of the mutated BarA proteins had poor complementation activity but could counteract the activity of the wild-type sensor in a dominant-negative fashion. These proteins carried point mutations in or near the recently identified HAMP linker, previously implicated in signal transduction between the periplasm and cytoplasm. This created sensor proteins with an impaired kinase activity and a net dephosphorylating activity. Using further site-directed mutagenesis of a HAMP linker-mutated protein, we could demonstrate that the phosphoaccepting aspartate 718 and histidine 861 are crucial for the dephosphorylating activity. Additional analysis of the HAMP linker-mutated BarA sensors demonstrated that a dephosphorylating activity can operate via phosphotransfer within a tripartite sensor dimer in vivo. This also means that a tripartite sensor can be arranged as a dimer even in the dephosphorylating mode.

Place, publisher, year, edition, pages
American Society for Microbiology , 2005. Vol. 187, no 21, 7317-7324 p.
National Category
Natural Sciences
Research subject
Natural sciences
Identifiers
URN: urn:nbn:se:his:diva-1798DOI: 10.1128/JB.187.21.7317-7324.2005ISI: 000232786100016PubMedID: 16237014Scopus ID: 2-s2.0-27144522004OAI: oai:DiVA.org:his-1798DiVA: diva2:32074
Available from: 2007-09-03 Created: 2007-09-03 Last updated: 2014-12-19Bibliographically approved

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CiteExportLink to record
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