Template-free ribosomal synthesis of polypeptides from aminoacyl-tRNA. Polyphenylalanine synthesis from phenylalanyl-tRNALys.
Misacylated phenylalanyl-tRNALys, just as lysyl-tRNALys, but not phenylalanyl-tRNAPhe, have been shown to serve as substrates for ribosomal synthesis of polypeptides (polyphenylalanine and polylysine, respectively) in the absence of a template polynucleotide (poly(A)). The conclusion was made that it is the structure of tRNA that determines the ability of the aminoacyl-tRNALys to participate in peptide elongation on ribosomes without codon-anticodon interactions.
D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000494:pharmacology; D010455:Peptides; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013698:Templates, Genetic
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D010455:Peptides; D012346:RNA, Transfer, Amino Acyl; C012001:polyphenylalanine; D008274:Magnesium