The L7/L12 proteins change their conformation upon interaction of EF-G with ribosomes.
The different functional complexes of ribosomes with elongation factor F (EF-G) were studied by digestion experiments with trypsin. It was found that upon interaction of EF-G with ribosomes the L7/L12 proteins are sensitive to trypsin and are trypsin resistant after dissociation of EF-G from ribosomes. The significance of conformational alterations in the L7/L12 and also in the other proteins in the translation process is discussed.
D001426:Bacterial Proteins / Q000378:metabolism; D004164:Diphosphonates / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D005672:Fusidic Acid / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006157:Guanosine Monophosphate / Q000031:analogs & derivatives / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives*; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000378:metabolism*; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology
D001426:Bacterial Proteins; D004164:Diphosphonates; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; D006153:Guanosine Diphosphate; C004805:5'-guanylylmethylenebisphosphonate; D005672:Fusidic Acid; C016700:ribosomal protein L7-L12; D006157:Guanosine Monophosphate; D006160:Guanosine Triphosphate; D014357:Trypsin