PMID:8104335

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Citation

Jones, CH, Pinkner, JS, Nicholes, AV, Slonim, LN, Abraham, SN and Hultgren, SJ (1993) FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria. Proc. Natl. Acad. Sci. U.S.A. 90:8397-401

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.

Links

PubMed PMC47363

Keywords

Adhesins, Escherichia coli; Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli Proteins; Fimbriae Proteins; Fimbriae, Bacterial/physiology; Genes, Bacterial; Genetic Complementation Test; Hemagglutination Tests; Hemagglutinins/metabolism; Molecular Sequence Data; Plasmids; Protein Structure, Secondary; Sequence Homology, Amino Acid

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