Immunocytochemical localization of the elongation factor Tu in E. coli cells.
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.
D002462:Cell Membrane / Q000032:analysis; D003593:Cytoplasm / Q000032:analysis; D004926:Escherichia coli / Q000648:ultrastructure*; D006046:Gold; D006651:Histocytochemistry; D007158:Immunologic Techniques; D008854:Microscopy, Electron; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000032:analysis*
D010445:Peptide Elongation Factors; D006046:Gold; D010444:Peptide Elongation Factor Tu