Document Detail

FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria.
MedLine Citation:
PMID:  8104335     Owner:  NLM     Status:  MEDLINE    
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.
C H Jones; J S Pinkner; A V Nicholes; L N Slonim; S N Abraham; S J Hultgren
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  90     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1993 Sep 
Date Detail:
Created Date:  1993-10-20     Completed Date:  1993-10-20     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8397-401     Citation Subset:  IM    
Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110.
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MeSH Terms
Adhesins, Escherichia coli
Amino Acid Sequence
Bacterial Outer Membrane Proteins / chemistry,  genetics,  metabolism*
Bacterial Proteins*
Escherichia coli / genetics,  physiology*
Escherichia coli Proteins*
Fimbriae Proteins*
Fimbriae, Bacterial / physiology*
Genes, Bacterial
Genetic Complementation Test
Hemagglutination Tests
Hemagglutinins / metabolism*
Molecular Sequence Data
Protein Structure, Secondary
Sequence Homology, Amino Acid
Grant Support
Reg. No./Substance:
0/Adhesins, Escherichia coli; 0/Bacterial Outer Membrane Proteins; 0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Hemagglutinins; 0/fimC protein, E coli; 147680-16-8/Fimbriae Proteins

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