Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes

Mol Microbiol. 1993 Oct;10(2):233-43. doi: 10.1111/j.1365-2958.1993.tb01949.x.


The Pseudomonas aeruginosa genes pilB-D and pilQ are necessary for the assembly of type 4 fimbriae. Homologues of these genes and of the subunit (pilin) gene have been described in various different bacterial species, but not always in association with type 4 fimbrial biosynthesis and function. Pil-like proteins are also involved in protein secretion, DNA transfer by conjugation and transformation, and morphogensis of filamentous bacteriophages. It seems likely that the Pil homologues function in the processing and export of proteins resembling type 4 fimbrial subunits, and in their organization into fimbrial-like structures. These may either be true type 4 fimbriae, or components of protein complexes which act in the transport of macromolecules (DNA or protein) into or out of the cell. Some PilB-like and PilQ-like proteins are apparently also involved in the assembly of non-type 4 polymeric structures (filamentous phage virions and conjugative pili). The diverse studies summarized in this review are providing insight into an extensive infrastructural system which appears to be utilized in the formation of a variety of cell surface-associated complexes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / metabolism*
  • Conjugation, Genetic
  • Endopeptidases*
  • Fimbriae Proteins*
  • Inovirus / growth & development
  • Molecular Sequence Data
  • Oxidoreductases*
  • Pili, Sex / classification
  • Pili, Sex / physiology*
  • Transformation, Genetic


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • pilC protein, Neisseria gonorrhoeae
  • pilQ protein, bacteria
  • Fimbriae Proteins
  • Oxidoreductases
  • pilB protein, Bacteria
  • Endopeptidases
  • prepilin peptidase protein, Bacteria