2004
DOI: 10.1128/jb.186.16.5321-5331.2004
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The Usher N Terminus Is the Initial Targeting Site for Chaperone-Subunit Complexes and Participates in Subsequent Pilus Biogenesis Events

Abstract: Pilus biogenesis on the surface of uropathogenic Escherichia coli requires the chaperone/usher pathway, a terminal branch of the general secretory pathway. In this pathway, periplasmic chaperone-subunit complexes target an outer membrane (OM) usher for subunit assembly into pili and secretion to the cell surface. The molecular mechanisms of protein secretion across the OM are not well understood. Mutagenesis of the P pilus usher PapC and the type 1 pilus usher FimD was undertaken to elucidate the initial stage… Show more

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Cited by 73 publications
(136 citation statements)
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“…The PapD-pilicide crystallographic data suggested that in the type 1 and P pilus systems pilicide 2c inhibits chaperone-subunit targeting to the usher or subsequent processing (16,17). This conclusion was supported by finding that R58A PapD was able to form stable chaperonesubunit complexes but was unable to assemble pili.…”
Section: Resultssupporting
confidence: 75%
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“…The PapD-pilicide crystallographic data suggested that in the type 1 and P pilus systems pilicide 2c inhibits chaperone-subunit targeting to the usher or subsequent processing (16,17). This conclusion was supported by finding that R58A PapD was able to form stable chaperonesubunit complexes but was unable to assemble pili.…”
Section: Resultssupporting
confidence: 75%
“…A ternary complex is formed that leads to uncapping of the chaperone, followed by incorporation of the subunit into the growing pilus (16,17). Assembly occurs by a process termed donor-strand exchange, in which the G1 ␤-strand of the chaperone is replaced by an N-terminal extension that is present on every subunit (14,15,18).…”
mentioning
confidence: 99%
“…The apparent affinity of the NTD-Plug complex for PapDG was two orders of magnitude lower than that for NTD alone and one order of magnitude lower than that for the Plug domain alone, suggesting that NTD in the context of a closed pore may be the initial targeting site for PapDG, thus initiating pilus formation, and that subsequent recruitment of chaperone-subunit complexes requires the NTD-Plug complex or the Plug domain alone. The PapC NTD has been implicated as the initial targeting site for chaperone-subunit complexes (26), and in the present study we show that NTD selectively binds to the PapDG chaperoneadhesin complex. However, the FimDCH crystal structure showed the chaperone-adhesin complex (FimCH) binding to the usher's CTDs (28).…”
Section: Resultsmentioning
confidence: 64%
“…A Plug-deleted PapC folds but does not assemble pili, suggesting that the Plug domain plays a direct role in catalyzing pilus biogenesis (29,30). Binding studies have suggested that the chaperone-adhesin complex is initially targeted to the NTD of PapC (26), and this is thought to activate the usher protein such that the β-sandwich Plug domain shifts from the channel, where it is located in the apo usher, to the periplasmic space, resulting in an open translocation pore (28). This affinity of the NTD for the chaperone-adhesin complex has also been shown for the type 1 pilus system (31).…”
mentioning
confidence: 99%
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