The role of protein L16 and its fragments in the peptidyltransferase activity of 50-S ribosomal subunits.
Two large polypeptide fragments of ribosomal protein L16 were obtained by limited hydrolysis with trypsin and chymotrypsin. The chymotryptic fragment, lacking nine N-terminal amino acids residues, is fully active in the restoration of the peptidyltransferase activity of the LiCl-stripped 50-S ribosomal subunits, whereas the tryptic fragment, lacking an additional six residues, is inactive. We also show that under the optimized ionic conditions protein L16 is not needed for the peptidyltransferase activity.
D000217:Acyltransferases / Q000378:metabolism*; D002918:Chymotrypsin; D004789:Enzyme Activation / Q000187:drug effects; D010446:Peptide Fragments / Q000494:pharmacology; D010458:Peptidyl Transferases / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000494:pharmacology*; D012270:Ribosomes / Q000201:enzymology*; D014357:Trypsin
D010446:Peptide Fragments; D012269:Ribosomal Proteins; C027937:ribosomal protein L16; D000217:Acyltransferases; D010458:Peptidyl Transferases; D002918:Chymotrypsin; D014357:Trypsin