The Usher N Terminus Is the Initial Targeting Site for Chaperone-Subunit Complexes and Participates in Subsequent Pilus Biogenesis Events

Ng, Tony W.; Akman, Leyla; Osisami, Mary; Thanassi, David G.

doi:10.1128/jb.188.6.2295.2006

Cited by 17 publications

(51 citation statements)

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“…The assignment of region 1 and 2 as the usher density and the extracellularly protruding adhesin, respectively, locates the remaining density region 3 to the periplasmic side of the complex ( Figure 5C). It is well established that the periplasmic side of the usher contains the N-and C-terminal domains as well as the last incorporated chaperone-subunit complex, which, in this case, is FimC:F (Hahn et al, 2002;Ng et al, 2004;Nishiyama et al, 2003Nishiyama et al, , 2005Saulino et al, 2000;Thanassi et al, 2002). This interpretation is further confirmed by the observation that binding of anti-His 6 antibodies followed by visualization by cryo-EM clearly locates FimC His in region 3 ( Figure S5B).…”

Section: Om Ushers Function As Asymmetric Twinned Poressupporting

confidence: 62%

“…The β-barrel closes in an end-to-end fashion and positions the N and C termini on the periplasmic side of the membrane. The N-and C-terminal globular domains will thus be juxtaposed and reside in the periplasm, consistent with their role in chaperone-subunit recruitment and adhesin-induced pore activation (Ng et al, 2004;Nishiyama et al, 2003;Saulino et al, 1998;Thanassi et al, 2002). The predicted middle domain (residues 257-332) is formed by a long sequence between strands β6 and β7 and consists of a six-stranded, βsandwich fold (strands βA-βF; Figure 2C).…”

Section: Structure Of the Usher Translocation Channelmentioning

confidence: 65%

“…OM ushers selectively recruit chaperone-bound subunits to the OM, facilitate their ordered polymerization, and translocate the nascent fiber across the OM. They comprise four predicted domains: an N-terminal periplasmic domain (~125 residues), a central β-barrel domain (predicted residues ~135 to ~640) interrupted by a middle domain (predicted residues ~220 to ~325), and a C-terminal periplasmic domain (~170 residues) ( Figure 1C) (Capitani et al, 2006;Ng et al, 2004;Nishiyama et al, 2003;Saulino et al, 1998;Thanassi et al, 2002). Chaperone-subunit recruitment occurs via the usher's Nterminal domain (Ng et al, 2004;Nishiyama et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…They comprise four predicted domains: an N-terminal periplasmic domain (~125 residues), a central β-barrel domain (predicted residues ~135 to ~640) interrupted by a middle domain (predicted residues ~220 to ~325), and a C-terminal periplasmic domain (~170 residues) ( Figure 1C) (Capitani et al, 2006;Ng et al, 2004;Nishiyama et al, 2003;Saulino et al, 1998;Thanassi et al, 2002). Chaperone-subunit recruitment occurs via the usher's Nterminal domain (Ng et al, 2004;Nishiyama et al, 2005). This domain discriminately recognizes different chaperone-subunit complexes by directly binding to the N-terminal domain of the periplasmic chaperone and part of the chaperone-bound subunit (Nishiyama et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Fiber Formation across the Bacterial Outer Membrane by the Chaperone/Usher Pathway

Remaut

Tang

Henderson

et al. 2008

Cell

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Gram-negative pathogens commonly exhibit adhesive pili on their surfaces that mediate specific attachment to the host. A major class of pili is assembled via the chaperone/usher pathway. Here, the structural basis for pilus fiber assembly and secretion performed by the outer membrane assembly platform--the usher--is revealed by the crystal structure of the translocation domain of the P pilus usher PapC and single particle cryo-electron microscopy imaging of the FimD usher bound to a translocating type 1 pilus assembly intermediate. These structures provide molecular snapshots of a twinned-pore translocation machinery in action. Unexpectedly, only one pore is used for secretion, while both usher protomers are used for chaperone-subunit complex recruitment. The translocating pore itself comprises 24 beta strands and is occluded by a folded plug domain, likely gated by a conformationally constrained beta-hairpin. These structures capture the secretion of a virulence factor across the outer membrane of gram-negative bacteria.

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Section: Om Ushers Function As Asymmetric Twinned Poressupporting

confidence: 62%

Section: Structure Of the Usher Translocation Channelmentioning

confidence: 65%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Fiber Formation across the Bacterial Outer Membrane by the Chaperone/Usher Pathway

Remaut

Tang

Henderson

et al. 2008

Cell

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202

291

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“…The chaperone‐adhesin complex is targeted to the usher first and opens the translocation pore (Saulino et al. , 1998; Ng et al. , 2004) through a conformational change that unplugs the translocation channel (Remaut et al.…”

Section: Classical Systemsmentioning

confidence: 99%

Biological ‘glue’ and ‘Velcro’: molecular tools for adhesion and biofilm formation in the hairy and gluey bug Pseudomonas aeruginosa

Giraud

Bernard

Ruer

et al. 2010

Environ Microbiol Rep

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Pseudomonas aeruginosa contains an extraordinarily large number of loci encoding systems facilitating a communal lifestyle and binding to supports of various natures. These P. aeruginosa systems are reviewed here and may be categorized as classical or non-classical systems. They highlight the panoply of strategies that this hairy and gluey bacterium has developed for dealing with the diverse environments with which it is faced during various types of infection, involving complex regulatory networks that have not yet been fully elucidated but several aspects of which are discussed here.

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Conformational Dynamics, Intramolecular Domain Conformation Signaling, and Activation of Apo-FimD Revealed by Single-Molecule Fluorescence Resonance Energy Transfer Studies

et al. 2019

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The chaperone–usher secretion pathway is a conserved bacterial protein secretion system dedicated to the biogenesis of adhesive fibers. Usher, a multidomain-containing outer membrane protein, plays a central role in this process by acting as a molecular machine that recruits different chaperone–subunit complexes, catalyzes subunit polymerization, and forms a channel for secretion of the assembled subunits. While recent crystal structural studies have greatly advanced our understanding of the structure and function of ushers, the overall architecture of the full-length apo-usher, the molecular events that dictate conformational changes in usher during pilus biogenesis, and its activation by the specific chaperone–adhesin complex remain largely elusive. Using single-molecule fluorescence resonance energy transfer studies, we found that the substrate-free usher FimD (apo-FimD) adopts a contracted conformation that is distinct from its substrate-bound states; both the N-terminal domain (NTD) and the C-terminal domain (CTD) of apo-FimD are highly dynamic, and FimD coordinates its domain conformational changes via intramolecular domain conformation signaling. By combining these studies with in vitro photo-cross-linking studies, we further show that only the chaperone-bound adhesin (FimC:FimH) can be transferred to the CTD, dislocates the plug domain, and triggers conformational changes in the remaining FimD domains. Taken together, these studies delineate an overall architecture of the full-length apo-FimD, provide detailed mechanic insight into the activation of apo-FimD, and explain why FimD could adjust its conformational states to perform multiple functions in each cycle of pilus subunit addition and ensure that pilus assembly proceeds progressively in a cellular energy-free environment.

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The Usher N Terminus Is the Initial Targeting Site for Chaperone-Subunit Complexes and Participates in Subsequent Pilus Biogenesis Events

Cited by 17 publications

References 0 publications

Fiber Formation across the Bacterial Outer Membrane by the Chaperone/Usher Pathway

Fiber Formation across the Bacterial Outer Membrane by the Chaperone/Usher Pathway

Biological ‘glue’ and ‘Velcro’: molecular tools for adhesion and biofilm formation in the hairy and gluey bug Pseudomonas aeruginosa

Conformational Dynamics, Intramolecular Domain Conformation Signaling, and Activation of Apo-FimD Revealed by Single-Molecule Fluorescence Resonance Energy Transfer Studies

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