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Template‐free ribosomal synthesis of polypeptides from aminoacyl‐tRNA
Author(s) -
Yusupova Gulnara Z.,
Belitsidezhda V.,
Spirin Alexander S.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81356-4
Subject(s) - polynucleotide , ribosome , aminoacyl trna , transfer rna , ribosomal rna , polylysine , biochemistry , biology , protein biosynthesis , peptide , chemistry , stereochemistry , rna , gene
Misacylated phenylalanyl‐tRNA Lys , just as lysyl‐tRNA Lys , but not phenylalanyl‐tRNA Phe , 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‐tRNA Lys to participate in peptide elongation on ribosomes without codon‐anticodon interactions.