FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria.

Journal Article (Journal Article)

Biogenesis of the type 1 pilus fiber in Escherichia coli requires the product of the fimC locus. We have demonstrated that FimC is a member of the periplasmic chaperone family. The deduced primary sequence of FimC shows a high degree of homology to PapD and fits well with the derived consensus sequence for periplasmic chaperones, predicting that it has an immunoglobulin-like topology. The chaperone activity of FimC was demonstrated by purifying a complex that FimC forms with the FimH adhesion. A fimC1 null allele could be complemented by the prototype member of the chaperone superfamily, PapD, resulting in the production of adhesive type 1 pili. The general mechanism of action of members of the chaperone superfamily was demonstrated by showing that the ability of PapD to assemble both P and type 1 pili was dependent on an invariant arginine residue (Arg-8), which forms part of a conserved subunit binding site in the cleft of PapD. We suggest that the conserved cleft is a subunit binding feature of all members of this protein family. These studies point out the general strategies used by Gram-negative bacteria to assemble adhesins into pilus fibers, allowing them to promote attachment to eukaryotic receptors.

Full Text

Duke Authors

Cited Authors

  • Jones, CH; Pinkner, JS; Nicholes, AV; Slonim, LN; Abraham, SN; Hultgren, SJ

Published Date

  • September 15, 1993

Published In

Volume / Issue

  • 90 / 18

Start / End Page

  • 8397 - 8401

PubMed ID

  • 8104335

Pubmed Central ID

  • PMC47363

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.90.18.8397


  • eng

Conference Location

  • United States