A lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation.
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Structural Mechanism of GAF-Regulated σ54 Activators from Aquifex aeolicusPspF-binding domain PspA1-144 and the PspA·F complex: New insights into the coiled-coil-dependent regulation of AAA+ proteinsCARF and WYL domains: ligand-binding regulators of prokaryotic defense systemsExperimental approaches for addressing fundamental biological questions in living, functioning cells with single molecule precision.Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein responseSignal sensory systems that impact σ⁵⁴ -dependent transcription.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.Measuring the stoichiometry of functional PspA complexes in living bacterial cells by single molecule photobleachingMembrane Stored Curvature Elastic Stress Modulates Recruitment of Maintenance Proteins PspA and Vipp1Dynamics and stoichiometry of a regulated enhancer-binding protein in live Escherichia coli cells.The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcriptionTranscription Regulation and Membrane Stress Management in Enterobacterial Pathogens.Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme.Evaluating the role of phage-shock protein A in Burkholderia pseudomallei.Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.Nitric oxide-responsive interdomain regulation targets the σ54-interaction surface in the enhancer binding protein NorRIn-depth profiling of the LiaR response of Bacillus subtilis.Dissipation of proton motive force is not sufficient to induce the phage shock protein response in Escherichia coli.A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis.Membrane chaperoning by members of the PspA/IM30 protein family.The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding.The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.Association of Mycobacterium proteins to lipid droplets.Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA.
P2860
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P2860
A lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
A lower-order oligomer form of ...... PspF for negative regulation.
@en
A lower-order oligomer form of phage shock protein A
@nl
type
label
A lower-order oligomer form of ...... PspF for negative regulation.
@en
A lower-order oligomer form of phage shock protein A
@nl
prefLabel
A lower-order oligomer form of ...... PspF for negative regulation.
@en
A lower-order oligomer form of phage shock protein A
@nl
P2860
P50
P1476
A lower-order oligomer form of ...... n PspF for negative regulation
@en
P2093
Martin Buck
Patricia C Burrows
P2860
P304
P356
10.1016/J.JMB.2009.09.055
P407
P577
2009-10-03T00:00:00Z