Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.
about
Structural analysis of a prototypical ATPase from the type III secretion systemMolecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pyloriAnalysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machineryProtein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Functional characterization of the type III secretion ATPase HrcN from the plant pathogen Xanthomonas campestris pv. vesicatoria.Crystallization and preliminary X-ray analysis of FliJ, a cytoplasmic component of the flagellar type III protein-export apparatus from Salmonella sp.Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domainsIdentification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo.A novel C-terminal region within the multicargo type III secretion chaperone CesT contributes to effector secretion.Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL.Type III secretion systems and bacterial flagella: insights into their function from structural similarities.Prokaryotic development: emerging insightsSynergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids.An escort mechanism for cycling of export chaperones during flagellum assembly.Self-assembly and type III protein export of the bacterial flagellum.Crystallization and preliminary X-ray analysis of the C-terminal cytoplasmic domain of FlhA, a membrane-protein subunit of the bacterial flagellar type III protein-export apparatusProcess of protein transport by the type III secretion systemCrystallization and preliminary X-ray analysis of Salmonella FliI, the ATPase component of the type III flagellar protein-export apparatus.The FliK protein and flagellar hook-length control.Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein exportQuantitative proteomic analysis reveals formation of an EscL-EscQ-EscN type III complex in enteropathogenic Escherichia coli.Functional Characterization of EscK (Orf4), a Sorting Platform Component of the Enteropathogenic Escherichia coli Injectisome.Secretin of the enteropathogenic Escherichia coli type III secretion system requires components of the type III apparatus for assembly and localization.The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH.Interactions of FliJ with the Salmonella type III flagellar export apparatusTranslocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli.Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO.Double hexameric ring assembly of the type III protein translocase ATPase HrcN.Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly.Crystallization and preliminary X-ray analysis of the FliH-FliI complex responsible for bacterial flagellar type III protein export.Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway.Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization.Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export.Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway.MxiN Differentially Regulates Monomeric and Oligomeric Species of the Shigella Type Three Secretion System ATPase Spa47.CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli.
P2860
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P2860
Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@en
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@nl
type
label
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@en
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@nl
prefLabel
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@en
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@nl
P2093
P2860
P1476
Intrinsic membrane targeting o ...... acidic phospholipids and FliH.
@en
P2093
Amanda J Ozin
Colin Hughes
Frédéric Auvray
Laurent Claret
P2860
P304
P356
10.1016/S0022-2836(02)00172-9
P407
P577
2002-05-01T00:00:00Z