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Immunocytochemical localization of the elongation factor Tu in E. coli cells
Author(s) -
Schilstra Maria J.,
Slot Jan W.,
van der Meide Peter H.,
Posthuma George,
Cremers Alfons F.M.,
Bosch Leendert
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80164-7
Subject(s) - periplasmic space , cytoplasm , elongation factor , cytoskeleton , ef tu , elongation , electron microscope , microbiology and biotechnology , inner membrane , bacterial outer membrane , biophysics , membrane , cell membrane , chemistry , biology , cell , crystallography , escherichia coli , biochemistry , rna , physics , gene , ribosome , materials science , ultimate tensile strength , optics , metallurgy
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 labellin 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.