Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG).
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Environmental Regulation of Yersinia PathophysiologyStress relief during host infection: The phage shock protein response supports bacterial virulence in various waysRecent findings about the Yersinia enterocolitica phage shock protein responseModulating Salmonella Typhimurium's Response to a Changing Environment through Bacterial Enhancer-Binding Proteins and the RpoN RegulonUse of a promiscuous, constitutively-active bacterial enhancer-binding protein to define the σ⁵⁴ (RpoN) regulon of Salmonella Typhimurium LT2.Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein responseGlobal analysis of extracytoplasmic stress signaling in Escherichia coli.The phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium.The evolution of the phage shock protein response system: interplay between protein function, genomic organization, and system function.6S RNA regulation of pspF transcription leads to altered cell survival at high pH.The putative thiosulfate sulfurtransferases PspE and GlpE contribute to virulence of Salmonella Typhimurium in the mouse model of systemic disease.Multiple promoters control expression of the Yersinia enterocolitica phage-shock-protein A (pspA) operon.The Yersinia enterocolitica phage shock proteins B and C can form homodimers and heterodimers in vivo with the possibility of close association between multiple domainsActivity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Regulation of bacterial virulence gene expression by cell envelope stress responses.Links between type III secretion and extracytoplasmic stress responses in YersiniaCharacterization of the Streptomyces lividans PspA response.6S RNA: a regulator of transcription.Dynamics and stoichiometry of a regulated enhancer-binding protein in live Escherichia coli cells.In vivo localizations of membrane stress controllers PspA and PspG in Escherichia coli.Analysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.Bacterial stressors in minimally processed food.The integration host factor (IHF) integrates stationary-phase and virulence gene expression in Salmonella enterica serovar Typhimurium.Global Gene-expression Analysis of the Response of Salmonella Enteritidis to Egg White Exposure Reveals Multiple Egg White-imposed Stress Responses.Transcription Regulation and Membrane Stress Management in Enterobacterial Pathogens.Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme.A transcriptional "Scream" early response of E. coli prey to predatory invasion by Bdellovibrio.Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the Yersinia enterocolitica Cytoplasmic Membrane.Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Biochemical and Genetic Characterization of PspE and GlpE, Two Single-domain Sulfurtransferases of Escherichia coli.PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response.Analysis of secretin-induced stress in Pseudomonas aeruginosa suggests prevention rather than response and identifies a novel protein involved in secretin function.Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.Global changes in cellular gene expression during bacteriophage PRD1 infection.Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator.Mutations in RNA Polymerase Bridge Helix and Switch Regions Affect Active-Site Networks and Transcript-Assisted Hydrolysis.Dissipation of proton motive force is not sufficient to induce the phage shock protein response in Escherichia coli.Molecular determinants for PspA-mediated repression of the AAA transcriptional activator PspF.A lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation.
P2860
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P2860
Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG).
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name
Identification of a new member ...... phage shock protein G (PspG).
@en
Identification of a new member ...... phage shock protein G (PspG).
@nl
type
label
Identification of a new member ...... phage shock protein G (PspG).
@en
Identification of a new member ...... phage shock protein G (PspG).
@nl
prefLabel
Identification of a new member ...... phage shock protein G (PspG).
@en
Identification of a new member ...... phage shock protein G (PspG).
@nl
P2093
P2860
P50
P356
P1476
Identification of a new member ...... e phage shock protein G (PspG)
@en
P2093
Arthur Thompson
Louise J Lloyd
Martin Buck
Matthew D Rolfe
Prasad Gyaneshwar
P2860
P304
55707-55714
P356
10.1074/JBC.M408994200
P407
P577
2004-10-13T00:00:00Z