PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response.
about
Recent findings about the Yersinia enterocolitica phage shock protein response'Big things in small packages: the genetics of filamentous phage and effects on fitness of their host'A large family of anti-activators accompanying XylS/AraC family regulatory proteinsChanges 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.Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocoliticaThe 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.Multiple promoters control expression of the Yersinia enterocolitica phage-shock-protein A (pspA) operon.A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscCThe 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.FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coliIdentification of YsaP, the Pilotin of the Yersinia enterocolitica Ysa Type III Secretion System.Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Links between type III secretion and extracytoplasmic stress responses in YersiniaPhage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress responseRegulation of the phage-shock-protein stress response in Yersinia enterocolitica.Analysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.The pneumococcal cell envelope stress-sensing system LiaFSR is activated by murein hydrolases and lipid II-interacting antibiotics.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.Physical, functional and conditional interactions between ArcAB and phage shock proteins upon secretin-induced stress in Escherichia coli.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.Elucidation of a protein-protein interaction network involved in Corynebacterium glutamicum cell wall biosynthesis as determined by bacterial two-hybrid analysis.The three-component system EsrISR regulates a cell envelope stress response in Corynebacterium glutamicum.Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA.
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P2860
PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response.
description
2006 nî lūn-bûn
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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2006年论文
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2006年论文
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name
PspB and PspC of Yersinia ente ...... phage-shock-protein response.
@en
type
label
PspB and PspC of Yersinia ente ...... phage-shock-protein response.
@en
prefLabel
PspB and PspC of Yersinia ente ...... phage-shock-protein response.
@en
P2860
P1476
PspB and PspC of Yersinia ente ...... phage-shock-protein response.
@en
P2093
Andrew J Darwin
Michelle E Maxson
P2860
P304
P356
10.1111/J.1365-2958.2006.05047.X
P407
P577
2006-03-01T00:00:00Z