Genetic and molecular characterization of flagellar assembly in Shewanella oneidensis

PLoS One. 2011;6(6):e21479. doi: 10.1371/journal.pone.0021479. Epub 2011 Jun 22.

Abstract

Shewanella oneidensis is a highly motile organism by virtue of a polar flagellum. Unlike most flagellated bacteria, it contains only one major chromosome segment encoding the components of the flagellum with the exception of the motor proteins. In this region, three genes encode flagellinsaccording to the original genome annotation. However, we find that only flaA and flaB encode functional filament subunits. Although these two genesare under the control of different promoters, they are actively transcribed and subsequently translated, producing a considerable number of flagellin proteins. Additionally, both flagellins are able to interact with their chaperon FliS and are subjected to feedback regulation. Furthermore, FlaA and FlaB are glycosylated by a pathwayinvolving a major glycosylating enzyme,PseB, in spite of the lack of the majority of theconsensus glycosylation sites. In conclusion, flagellar assembly in S. oneidensis has novel features despite the conservation of homologous genes across taxa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Computational Biology
  • Feedback, Physiological
  • Flagella / genetics*
  • Flagella / metabolism*
  • Flagella / ultrastructure
  • Genes, Bacterial / genetics
  • Genetic Complementation Test
  • Glycosylation
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Movement
  • Mutation / genetics
  • Plasmids / genetics
  • Promoter Regions, Genetic / genetics
  • Protein Binding
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism
  • Sequence Alignment
  • Shewanella / genetics*
  • Shewanella / metabolism*
  • Shewanella / ultrastructure

Substances

  • Bacterial Proteins
  • Molecular Chaperones
  • Protein Subunits