Variable symmetry in Salmonella typhimurium flagellar motors

Biophys J. 2003 Jan;84(1):571-7. doi: 10.1016/S0006-3495(03)74877-2.

Abstract

Electron cryomicroscopy of rotor complexes of the Salmonella typhimurium flagellar motor, overproduced in a nonmotile Escherichia coli host, has revealed a variation in subunit symmetry of the cytoplasmic ring (C ring) module. C rings with subunit symmetries ranging from 31 to 38 were found. They formed a Gaussian distribution around a mean between 34 and 35, a similar number to that determined for native C rings. C-ring diameter scaled with the number of subunits, indicating that the elliptical-shaped subunits maintained constant intersubunit spacing. Taken together with evidence that the M ring does not correspondingly increase in size, this finding indicates that rotor assembly does not require strict stoichiometric interactions between the M- and C-ring subunits. Implications for motor function are discussed.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / ultrastructure
  • Cryoelectron Microscopy / methods
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Flagella / chemistry*
  • Flagella / ultrastructure*
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / ultrastructure
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / ultrastructure*
  • Protein Conformation
  • Protein Subunits / chemistry
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / ultrastructure
  • Salmonella typhimurium / chemistry*
  • Salmonella typhimurium / ultrastructure

Substances

  • Bacterial Proteins
  • FliN protein, Bacteria
  • Flif protein, Bacteria
  • Flig protein, Bacteria
  • Membrane Proteins
  • Molecular Motor Proteins
  • Protein Subunits
  • Recombinant Proteins
  • FliM protein, Bacteria