Comparison of ribosomes from Coxiella burnetii and Escherichia coli by gel electrophoresis, protein synthesis, and immunological techniques.
Ribosomes and postribiosomal supernatant fluid (S-100) were isolated from Coxiella burnetii. The ribosomes functioned in polyuridylic acid-directed polyphenylalanine synthesis in the presence of S-100 from either C. burnetii or Escherichia coli. C. burnetii S-100 promoted translation with E. coli ribosomes. Antisera against E. coli elongation factor G and ribosomal proteins L7/L12 cross-reacted with rickettsial S-100 and ribosomes, respectively. Ribosomal proteins were analyzed by two-dimensional gel electrophoresis.
D001426:Bacterial Proteins / Q000032:analysis* / Q000096:biosynthesis; D003381:Coxiella / Q000648:ultrastructure*; D004926:Escherichia coli / Q000648:ultrastructure*; D014176:Protein Biosynthesis; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000032:analysis* / Q000502:physiology; D013045:Species Specificity
D001426:Bacterial Proteins; D012269:Ribosomal Proteins