Template-free ribosomal synthesis of polypeptides from aminoacyl-tRNAs : polyphenylalanine synthesis from phenylalanyl-tRNALys

Authors

  • G. Zh. Yusupova (Tnalina) Institute of Protein Research, Academy of Sciences of the USSR Pushchino, Moscow Region, USSR Author
  • N. V. Belitsina A. N. Bakh Institute of Biochemistry, Academy of Sciences of the USSR Moscow, USSR Author
  • A. S. Spirin Institute of Protein Research, Academy of Sciences of the USSR Pushchino, Moscow Region, USSR Author

DOI:

https://doi.org/10.7124/bc.0001B2

Abstract

Misacylated phenylalanyl-tRNALys, similar to lysyl-tRNALys, but not phenylalanyl-tRNAPhe, is able to serve as a substrate for ribosomal synthesis of polypeptides (poly-phenylalanine and polylysine, respectively) in the absence of a template polynucleotide (poly(A)). Thus, it is the structure of tRNA that determines the ability of the amino-acyl-tRNALys to participate in the peptide elongation on ribosomes without codon-anti-codon interactions.

References

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Published

1986-07-20

Issue

Section

Structure and Function of Biopolymers