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Journal of bacteriology v.199 no.5, 2017년, pp.e00746-16 - e00746-16   SCI SCIE
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Conserved ABC Transport System Regulated by the General Stress Response Pathways of Alpha- and Gammaproteobacteria

Herrou, Julien (Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA ) ; Willett, Jonathan W. (Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA ) ; Czyż, Daniel M. (Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA ) ; Babnigg, Gyorgy (Argonne National Laboratory, Argonne, Illinois, USA ) ; Kim, Youngchang (Argonne National Laboratory, Argonne, Illinois, USA ) ; Crosson, Sean (Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA ) ;
  • 초록  

    Brucella abortus σ E1 is an EcfG family sigma factor that regulates the transcription of dozens of genes in response to diverse stress conditions and is required for maintenance of chronic infection in a mouse model. A putative ATP-binding cassette transporter operon, bab1_0223-bab1_0226 , is among the most highly activated gene sets in the σ E1 regulon. The proteins encoded by the operon resemble quaternary ammonium-compatible solute importers but are most similar in sequence to the broadly conserved YehZYXW system, which remains largely uncharacterized. Transcription of yehZYXW is activated by the general stress sigma factor σ S in Enterobacteriaceae , which suggests a functional role for this transport system in bacterial stress response across the classes Alphaproteobacteria and Gammaproteobacteria . We present evidence that B. abortus YehZYXW does not function as an importer of known compatible solutes under physiological conditions and does not contribute to the virulence defect of a σ E1 -null strain. The sole in vitro phenotype associated with genetic disruption of this putative transport system is reduced growth in the presence of high Li + ion concentrations. A crystal structure of B. abortus YehZ revealed a class II periplasmic binding protein fold with significant structural homology to Archaeoglobus fulgidus ProX, which binds glycine betaine. However, the structure of the YehZ ligand-binding pocket is incompatible with high-affinity binding to glycine betaine. This is consistent with weak measured binding of YehZ to glycine betaine and related compatible solutes. We conclude that YehZYXW is a conserved, stress-regulated transport system that is phylogenetically and functionally distinct from quaternary ammonium-compatible solute importers. IMPORTANCE Brucella abortus σ E1 regulates transcription in response to stressors encountered in its mammalian host and is necessary for maintenance of chronic infection in a mouse model. The functions of the majority of genes regulated by σ E1 remain undefined. We present a functional/structural analysis of a conserved putative membrane transport system (YehZYXW) whose expression is strongly activated by σ E1 . Though annotated as a quaternary ammonium osmolyte uptake system, experimental physiological studies and measured ligand-binding properties of the periplasmic binding protein (PBP), YehZ, are inconsistent with this function. A crystal structure of B. abortus YehZ provides molecular insight into differences between bona fide quaternary ammonium osmolyte importers and YehZ-related proteins, which form a distinct phylogenetic and functional group of PBPs.


  • 주제어

    Alphaproteobacteria .   general stress response .   EcfG .   lithium .   sigma factor .   ABC transporter .   RpoS .   YehZ .   YehZYXW.  

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