Iodination of Escherichia coli ribosomal protein L18 abolishes its 5 S RNA binding activity.
Iodination of Escherichia coli ribosomal protein L18 inactivated the 5 S RNA binding activity of the protein. Complete activity loss occurred at a 4-fold molar excess of iodine to L18. Tyrosine was found to be the reactive amino acid. L18, prebound to 5 S RNA, was inactivated at a much slower rate than unbound L18. Treatment of L18 with tetranitromethane also resulted in an inactivation of the protein. However, much larger amounts of tetranitromethane, compared to iodine, were necessary to achieve inactivation (50% activity loss at a 600-fold molar excess of tetranitromethane to L18).
D002352:Carrier Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D007455:Iodine; D007700:Kinetics; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism*; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013774:Tetranitromethane
D002352:Carrier Proteins; D012335:RNA, Ribosomal; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C029609:ribosomal protein L18; D007455:Iodine; D013774:Tetranitromethane