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  • 1
    ISSN: 1617-4623
    Keywords: Ribosomal topography ; Ribosomal protein L27 ; Immuno-electron microscopy ; Peptidyl transferase centre
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Protein L27 has been localized on the ribosomal surface by immuno-electron microscopy by using antibodies specific for Escherichia coli L27, and by reconstituting 50 S subunits from an E. coli mutant, which lacks protein L27, with the homologous protein from Bacillus subtilis and using antibodies specific for the B. subtilis protein. With both approaches, protein L27 has been located at the base of the central protuberance at the interface side of the 50 S particle and thus in proximity to the peptidyl transferase centre. The immuno-electron microscopic data also suggest that the interface region of the 50 S particle is not as flat as most of the proposed three-dimensional models suggest, but instead there is a significant depression.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Ribosome topography ; Ribosomal proteins-50S ; subunit ; Immuno-electron microscopy ; Antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.
    Type of Medium: Electronic Resource
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