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Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuni
dc.contributor.authorElliott, Kathryn T.en_US
dc.contributor.authorDiRita, Victor J.en_US
dc.date.accessioned2010-06-01T22:11:49Z
dc.date.available2010-06-01T22:11:49Z
dc.date.issued2008-09en_US
dc.identifier.citationElliott, Kathryn T.; DiRita, Victor J. (2008). "Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuni ." Molecular Microbiology 69(5): 1091-1103. <http://hdl.handle.net/2027.42/75215>en_US
dc.identifier.issn0950-382Xen_US
dc.identifier.issn1365-2958en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/75215
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=18631239&dopt=citationen_US
dc.description.abstractThe energy taxis receptor Aer, in Escherichia coli , senses changes in the redox state of the electron transport system via an flavin adenine dinucleotide cofactor bound to a PAS domain. The PAS domain (a sensory domain named after three proteins P er, A RNT and S im, where it was first identified) is thought to interact directly with the Aer HAMP domain to transmit this signal to the highly conserved domain (HCD) found in chemotaxis receptors. An apparent energy taxis system in Campylobacter jejuni is composed of two proteins, CetA and CetB, that have the domains of Aer divided between them. CetB has a PAS domain, while CetA has a predicted transmembrane region, HAMP domain and the HCD. In this study, we examined the expression of cetA and cetB and the biochemical properties of the proteins they encode. cetA and cetB are co-transcribed independently of the flagellar regulon. CetA has two transmembrane helices in a helical hairpin while CetB is a peripheral membrane protein tightly associated with the membrane. CetB levels are CetA dependent. Additionally, we demonstrated that both CetA and CetB participate in complexes, including a likely CetB dimer and a complex that may include both CetA and CetB. This study provides a foundation for further characterization of signal transduction mechanisms within CetA/CetB.en_US
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dc.format.extent3109 bytes
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dc.publisherBlackwell Publishing Ltden_US
dc.rightsJournal compilation © 2008 Blackwell Publishingen_US
dc.titleCharacterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejunien_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumUnit for Laboratory Animal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.en_US
dc.contributor.affiliationotherDepartment of Microbiology and Immunology anden_US
dc.identifier.pmid18631239en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/75215/1/j.1365-2958.2008.06357.x.pdf
dc.identifier.doi10.1111/j.1365-2958.2008.06357.xen_US
dc.identifier.sourceMolecular Microbiologyen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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