Immunocytochemical localization of the elongation factor Tu in E. coli cells

FEBS Lett. 1984 Jan 9;165(2):175-9. doi: 10.1016/0014-5793(84)80164-7.

Abstract

The localization of the elongation factor Tu (EF-Tu) in ultrathin cryosections of E. coli cells was determined with the electron microscope using a highly specific immunological labelling technique. EF-Tu is distributed almost homogeneously throughout the cytoplasm. Although it has often been suggested that EF-Tu could be part of a putative prokaryotic cytoskeleton, we did not find any evidence for supramolecular assemblies, such as fibres or filaments, containing a large amount of EF-Tu. EF-Tu was not observed in association with the outer cell membrane and periplasmic space. A topological relationship with the inner membrane is not apparent in our micrographs. In cells in which the EF-Tu level is raised significantly, the protein piles up in discrete cell regions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / analysis
  • Cytoplasm / analysis
  • Escherichia coli / ultrastructure*
  • Gold
  • Histocytochemistry
  • Immunologic Techniques
  • Microscopy, Electron
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors / analysis*

Substances

  • Peptide Elongation Factors
  • Gold
  • Peptide Elongation Factor Tu