Functional implication of the sole arginine residue of ribosomal proteins L7/L12.
Modification of the only arginine residue present in proteins L7/L12 from Escherichia coli with phenylglyoxal, 2,3-butanedione and 1,2-cyclohexanedione is accompanied by functional alterations. The capacity of these proteins to promote polyphenylalanine synthesis and elongation factor G-dependent hydrolysis of GTP in L7/L12-depleted ribosomal cores is significantly decreased (more than 50%) on modification. Incubation of the butanedione- and cyclohexanedione-modified L7/L12 under regenerating conditions is accompanied by recovery of the original activity in polyphenylalanine synthesis. These results and the conservation of the arginine residue in eubacterial L7/L12-type proteins point to the functional implication of this arginine residue.
D000595:Amino Acid Sequence; D001120:Arginine; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D010452:Peptide Biosynthesis; D010455:Peptides; D012269:Ribosomal Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D010455:Peptides; D012269:Ribosomal Proteins; D006153:Guanosine Diphosphate; C012001:polyphenylalanine; D006160:Guanosine Triphosphate; D001120:Arginine