Implication of arginyl residues in mRNA binding to ribosomes.
Modification of Escherichia coli robosomes with phenylglyoxal and butanedione, protein reagents specific for arginyl residues, inactivates polypeptide polymerization, assayed as poly(U)-dependent polyphenylalanine synthesis, and the binding of poly(U). Inactivation is produced by modification of the 30-S subunit. Both the RNA and the protein moieties of 30-S subunits are modified by phenylglyoxal, and modification of either of them is accompanied by inactivation of polypeptide synthesis. Modification of only the split proteins released from 30-S subunits by prolonged dialysis against a low-ionic-strength buffer, which contain mainly protein S1, produces inhibition of poly(U) binding and inactivation of polypeptide synthesis. Amino acid analysis of the modified split proteins showed a significant modifications of arginyl residues. These results indicate that the arginyl residues of a few 30-S proteins might be important in the interaction between mRNA and the 30-S subunit, which agrees with the general role assigned to the arginyl residues of proteins as the positively charged recognition site for anionic ligands.
D001120:Arginine / Q000037:antagonists & inhibitors / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D003931:Diacetyl / Q000494:pharmacology; D004926:Escherichia coli; D010658:Phenylglyoxal / Q000494:pharmacology; D011072:Poly U / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D012329:RNA, Bacterial / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger; D012269:Ribosomal Proteins; D011072:Poly U; D001120:Arginine; D003931:Diacetyl; D010658:Phenylglyoxal