The localization of protein L19 on the surface of 50 S subunits of Escherichia coli aided by the use of mutants lacking protein L19.
Three independently isolated mutants of Escherichia coli which apparently lacked protein L19 on their ribosomes, as judged by two-dimensional gels, were analyzed by a range of immunological tests to determine if the protein was indeed lacking. In two of the three, all the tests indicated that protein L19 was absent from both ribosome and supernatant. In the third, a drastically altered form of protein L19 was present on the ribosome. Electron micrographs of ribosomes obtained from the mutants were indistinguishable from those of wild type strains. The location of ribosomal protein L19 on the surface of the large subunit was determined. It was situated at the base of the 50 S particle facing the small subunit, on the side where the rod like appendage originates.
D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics* / Q000648:ultrastructure; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D008854:Microscopy, Electron; D008961:Models, Structural; D009154:Mutation; D012269:Ribosomal Proteins / Q000032:analysis* / Q000235:genetics; D012270:Ribosomes / Q000648:ultrastructure*
D012269:Ribosomal Proteins