title: Involvement of AtoSC two-component system in Escherichia coli flagellar regulon.
abstract: The AtoSC two-component system in Escherichia coli is a key regulator of many physiological processes. We report here the contribution of AtoSC in E. coli motility and chemotaxis. AtoSC locus deletion in ΔatoSC cells renders cells not motile or responsive against any chemoattractant or repellent independently of the AtoSC inducer's presence. AtoSC expression through plasmid complemented the ΔatoSC phenotype. Cells expressing either AtoS or AtoC demonstrated analogous motility and chemotactic phenotypes as ΔatoSC cells, independently of AtoSC inducer's presence. Mutations of AtoC phosphate-acceptor sites diminished or abrogated E. coli chemotaxis. trAtoC, the AtoC constitutive active form which lacks its receiver domain, up-regulated E. coli motility. AtoSC enhanced the transcription of the flhDC and fliAZY operons and to a lesser extent of the flgBCDEFGHIJKL operon. The AtoSC-mediated regulation of motility and chemotactic response required also the expression of the CheAY system. The AtoSC inducers enhanced the AtoSC-mediated motility and chemotaxis. Acetoacetate or spermidine further promoted the responses of only AtoSC-expressing cells, while Ca(2+) demonstrated its effects independently of AtoSC. Histamine regulated bacterial chemotaxis only in atoSC                         (+) cells in a concentration-dependent manner while reversed the AtoSC-mediated effects when added at high concentrations. The trAtoC-controlled motility effects were enhanced by acetoacetate or spermidine, but not by histamine. These data reveal that AtoSC system regulates the motility and chemotaxis of E. coli, participating in the transcriptional induction of the main promoters of the chemotactic regulon and modifying the motility and chemotactic phenotypes in an induction-dependent mechanism.
authors.affiliation: Laboratory of Biochemistry, Department of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece. mtheod80@yahoo.com
authors.forename: Marina C
authors.initials: MC
authors.lastname: Theodorou
authors.forename: Evaggelos C
authors.initials: EC
authors.lastname: Theodorou
authors.forename: Dimitrios A
authors.initials: DA
authors.lastname: Kyriakidis
mesh_terms: D000090:Acetoacetates / Q000737:chemistry; D019943:Amino Acid Substitution; D001224:Aspartic Acid / Q000737:chemistry; D002118:Calcium / Q000737:chemistry; D002630:Chemotactic Factors / Q000737:chemistry; D002633:Chemotaxis / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000235:genetics* / Q000378:metabolism; D005407:Flagella; D015964:Gene Expression Regulation, Bacterial; D055786:Gene Knockout Techniques; D005990:Glycerol / Q000737:chemistry; D006632:Histamine / Q000737:chemistry; D009876:Operon; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D018085:Regulon; D012694:Serine / Q000737:chemistry; D013095:Spermidine / Q000737:chemistry
chemical_list: D000090:Acetoacetates; C505587:AtoC protein, E coli; D002630:Chemotactic Factors; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D001224:Aspartic Acid; D012694:Serine; C016635:acetoacetic acid; D006632:Histamine; D011494:Protein Kinases; C505586:AtoS protein, E coli; D005990:Glycerol; D002118:Calcium; D013095:Spermidine