Interactions between phage-shock proteins in Escherichia coli.
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PspF-binding domain PspA1-144 and the PspA·F complex: New insights into the coiled-coil-dependent regulation of AAA+ proteinsChanges in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein responsePhage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway.The phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium.Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocoliticaIdentification of inducers of the Yersinia enterocolitica phage shock protein system and comparison to the regulation of the RpoE and Cpx extracytoplasmic stress responses.RtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system.6S RNA regulation of pspF transcription leads to altered cell survival at high pH.Regulation of LiaRS-dependent gene expression in bacillus subtilis: identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system.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.PspG, a new member of the Yersinia enterocolitica phage shock protein regulonPhage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Phage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress responseThe Escherichia coli peripheral inner membrane proteome.Characterization of the Streptomyces lividans PspA response.Regulation of the phage-shock-protein stress response in Yersinia enterocolitica.The LiaFSR system regulates the cell envelope stress response in Streptococcus mutans.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.The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcriptionTranscription Regulation and Membrane Stress Management in Enterobacterial Pathogens.Secretion defects that activate the phage shock response of Escherichia coli.A novel family of Escherichia coli toxin-antitoxin gene pairs.Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the Yersinia enterocolitica Cytoplasmic Membrane.J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1.Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Physical, functional and conditional interactions between ArcAB and phage shock proteins upon secretin-induced stress in Escherichia coli.PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response.Role of the extracytoplasmic function protein family sigma factor RpoE in metal resistance of Escherichia coliProperties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.In-depth profiling of the LiaR response of Bacillus subtilis.A lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation.PspA can form large scaffolds in Escherichia coli.The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding.Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.The three-component system EsrISR regulates a cell envelope stress response in Corynebacterium glutamicum.Escherichia coli phage-shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes.
P2860
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P2860
Interactions between phage-shock proteins in Escherichia coli.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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name
Interactions between phage-shock proteins in Escherichia coli.
@en
Interactions between phage-shock proteins in Escherichia coli.
@nl
type
label
Interactions between phage-shock proteins in Escherichia coli.
@en
Interactions between phage-shock proteins in Escherichia coli.
@nl
prefLabel
Interactions between phage-shock proteins in Escherichia coli.
@en
Interactions between phage-shock proteins in Escherichia coli.
@nl
P2093
P2860
P1476
Interactions between phage-shock proteins in Escherichia coli.
@en
P2093
Hendrik Adams
Jan Tommassen
Rolf Boesten
Wieke Teertstra
P2860
P304
P356
10.1128/JB.185.4.1174-1180.2003
P407
P577
2003-02-01T00:00:00Z