Amino acids responsible for flagellar shape are distributed in terminal regions of flagellin

J Mol Biol. 1991 Jun 5;219(3):471-80. doi: 10.1016/0022-2836(91)90187-b.

Abstract

The shape of the flagellar filaments of the bacterium Salmonella typhimurium under ordinary conditions is a left-handed helix. In addition to the normal wild-type filament, non-helical (i.e. straight), right-handed helical (early), or circular (semi-coiled and coiled) filaments and filament with small amplitude (fl-type) have been found in mutants or in filaments reconstituted in vitro. We analysed wild-type flagellin and flagellins from 17 flagellar-shape mutants (6 with straight filaments, 6 with curly filaments, 4 with coiled filaments and 1 with fl-type filament) by amino acid sequencing to identify the mutational sites. All mutant flagellins except that of the fl-type filament had single mutations; the fl-type flagellin had two mutations in the molecule. The sites of these mutations were localized in alpha-helical segments of the terminal regions of flagellin. A possible mechanism of the polymorphism of the flagellar filament is discussed.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Cyanogen Bromide
  • Flagella / ultrastructure*
  • Flagellin / genetics*
  • Flagellin / isolation & purification
  • Flagellin / ultrastructure
  • Molecular Sequence Data
  • Peptide Fragments / isolation & purification
  • Peptide Mapping
  • Protein Conformation
  • Salmonella typhimurium / genetics*
  • Salmonella typhimurium / ultrastructure
  • Trypsin

Substances

  • Peptide Fragments
  • Flagellin
  • Trypsin
  • Cyanogen Bromide