Further evidence for the participation of proteins S 3, S 14 and S 19 in tRNA binding to E. coli 30 S subunits.
Previous studies have shown that iodination of 30 S subunits causes inactivation for both enzymatic fMet-tRNA and non-enzymatic phe-tRNA binding activities. This inactivation was shown to be due to the modification of three to five ribosomal proteins [1]. In this report the role of these proteins in tRNA binding activity has been further studied. Purified ribosomal proteins, isolated from modified subunits, are re-assembled into otherwise unmodified 30 S ribosomes and assayed for tRNA binding capacity. The presence of modified S 3, S 14 and S 19 (S 15) in the reconstituted particle results in substantial reduction of both fMet-tRNA and phe-tRNA binding activities. This reduction in tRNA binding activity does not appear to be due to an assembly defect.
D001665:Binding Sites; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D004926:Escherichia coli / Q000378:metabolism*; D008715:Methionine; D008970:Molecular Weight; D010649:Phenylalanine; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure
D012269:Ribosomal Proteins; D010649:Phenylalanine; D012343:RNA, Transfer; D008715:Methionine