Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek

Microbiol Mol Biol Rev. 2007 Dec;71(4):551-75. doi: 10.1128/MMBR.00014-07.

Abstract

Many Proteobacteria use the chaperone/usher pathway to assemble proteinaceous filaments on the bacterial surface. These filaments can curl into fimbrial or nonfimbrial surface structures (e.g., a capsule or spore coat). This article reviews the phylogeny of operons belonging to the chaperone/usher assembly class to explore the utility of establishing a scheme for subdividing them into clades of phylogenetically related gene clusters. Based on usher amino acid sequence comparisons, our analysis shows that the chaperone/usher assembly class is subdivided into six major phylogenetic clades, which we have termed alpha-, beta-, gamma-, kappa-, pi-, and sigma-fimbriae. Members of each clade share related operon structures and encode fimbrial subunits with similar protein domains. The proposed classification system offers a simple and convenient method for assigning newly discovered chaperone/usher systems to one of the six major phylogenetic groups.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Evolution, Molecular
  • Fimbriae, Bacterial / classification*
  • Fimbriae, Bacterial / genetics
  • Fimbriae, Bacterial / metabolism
  • Genes, Bacterial
  • Molecular Chaperones / genetics*
  • Molecular Chaperones / metabolism
  • Multigene Family
  • Operon*
  • Phylogeny
  • Proteobacteria / genetics*
  • Proteobacteria / metabolism*

Substances

  • Bacterial Proteins
  • Molecular Chaperones