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. 1993 Sep 15;90(18):8397–8401. doi: 10.1073/pnas.90.18.8397

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

C H Jones 1, J S Pinkner 1, A V Nicholes 1, L N Slonim 1, S N Abraham 1, S J Hultgren 1
PMCID: PMC47363  PMID: 8104335

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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