title: The glutamate-dependent acid resistance system in Escherichia coli: essential and dual role of the His-Asp phosphorelay RcsCDB/AF.
abstract: The RcsCDB signal transduction system is an atypical His-Asp phosphorelay. Notably, the response regulator RcsB can be activated either by phosphorylation through the RcsCD pathway or by an accessory cofactor RcsA. Although conserved in Enterobacteriaceae, the role of this system in adaptation to environmental stress conditions is largely unknown. This study reveals that the response regulator RcsB is essential to glutamate-dependent acid resistance, a condition pertinent to the lifestyle of Escherichia coli. The requirement for RcsB is independent of its activation by either the RcsCD or the RcsA pathway. The basal activity of RcsB appears to be necessary and sufficient for acid resistance. The sensitivity of the rcsB strain to low pH is correlated to a strong reduction of the expression of the glutamate decarboxylase genes, gadA and gadB, during the stationary phase of growth. This effect on gadA/B expression is not mediated by the general stress sigma factor RpoS, but does require a functional gadE allele and the previously identified GadE box. Therefore activation of gadAB expression and acid resistance absolutely requires both GadE and RcsB. In contrast, an increase in RcsB activity through the activation of the RcsCD phosphorelay or the RcsA pathway or through overproduction of the protein leads to general repression of the expression of the gad genes and a corresponding reduction in acid resistance.
authors.affiliation: Laboratoire de Microbiologie et de Génétique Moléculaire, Centre National de la Recherche Scientifique, Université Paul Sabatier, 118 Route de Narbonne, 31062 Toulouse, France.
authors.forename: Marie-Pierre
authors.initials: MP
authors.lastname: Castanié-Cornet
authors.forename: Hélène
authors.initials: H
authors.lastname: Treffandier
authors.forename: Anne
authors.initials: A
authors.lastname: Francez-Charlot
authors.forename: Claude
authors.initials: C
authors.lastname: Gutierrez
authors.forename: Kaymeuang
authors.initials: K
authors.lastname: Cam
mesh_terms: D000143:Acids / Q000494:pharmacology*; D000222:Adaptation, Physiological; D001224:Aspartic Acid / Q000378:metabolism; D024881:Drug Resistance, Bacterial; D004926:Escherichia coli / Q000187:drug effects* / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics* / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial; D005968:Glutamate Decarboxylase / Q000235:genetics; D006639:Histidine / Q000378:metabolism; D009097:Multienzyme Complexes / Q000235:genetics*; D010749:Phosphoprotein Phosphatases / Q000235:genetics*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000235:genetics*; D011494:Protein Kinases / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics / Q000502:physiology*
chemical_list: D000143:Acids; D029968:Escherichia coli Proteins; C479562:GadE protein, E coli; D009097:Multienzyme Complexes; C489568:RcsB protein, E coli; D014157:Transcription Factors; C489728:rcsC protein, E coli; C078611:rcsF protein, E coli; C067572:RcsA protein, E coli; D001224:Aspartic Acid; D006639:Histidine; D010770:Phosphotransferases; D011494:Protein Kinases; C434271:rcsD protein, E coli; D010749:Phosphoprotein Phosphatases; D005968:Glutamate Decarboxylase