Ribosomal protein L16 binds to the 3'-end of transfer RNA.
Escherichia coli 50 S ribosomal subunits were reconstituted with and without protein L16 present. The latter particles, although active in puromycin reaction, were unable to use CACCA-Phe as an acceptor substrate. We also found that L16 interacts directly with this oligonucleotide and, in the complex with tRNA, protects its 3'-end from pancreatic ribonuclease digestion. We suggest that the role of L16 is in the fixation of the aminoacyl stem of tRNA to the ribosome at its A-site.
D001665:Binding Sites; D004926:Escherichia coli; D012343:RNA, Transfer / Q000378:metabolism*; D012260:Ribonucleases; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D012269:Ribosomal Proteins; D012343:RNA, Transfer; D012260:Ribonucleases