The interaction of ribosomal protein L16 and its fragments with tRNA.
Two large proteolytic fragments of Escherichia coli 50 S ribosomal subunit protein L16 were generated by limited hydrolysis with chymotrypsin (missing 9 N-terminal amino acids) and trypsin (missing 16 N-terminal amino acids). It was found that while intact L16 and its chymotryptic fragment both interact with tRNA (Kd = 5.4 x 10(-7) M), the tryptic fragment does not. These results are interpreted in terms of possible significance of the residues 10-16 in the peptidyl transferase activity.
D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000302:isolation & purification; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D012261:Ribonucleoproteins; D012269:Ribosomal Proteins; C027937:ribosomal protein L16; D012343:RNA, Transfer