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Biomolecules. 2019 Oct 8;9(10). pii: E588. doi: 10.3390/biom9100588.

The Reverse Side of a Coin: "Factor-Free" Ribosomal Protein Synthesis In Vitro is a Consequence of the In Vivo Proofreading Mechanism.

Author information

1
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. afinkel@vega.protres.ru.
2
Biology Department, Lomonosov Moscow State University, 119192 Moscow, Russia. afinkel@vega.protres.ru.

Abstract

This paper elucidates a close connection between two well-known facts that until now have seemed independent: (i) the quality control ("proofreading") of the emerging amino acid sequence, occurring during the normal, elongation-factor-dependent ribosomal biosynthesis, which is performed by removing those Aa-tRNAs (aminoacyl tRNAs) whose anticodons are not complementary to the exhibited mRNA codons, and (ii) the in vitro discovered existence of the factor-free ribosomal synthesis of polypeptides. It is shown that a biological role of proofreading is played by a process that is exactly opposite to the step of factor-free binding of Aa-tRNA to the ribosome-exposed mRNA: a factor-free removal of that Aa-tRNA whose anticodon is not complementary to the ribosome-exhibited mRNA codon.

KEYWORDS:

EFTu; GTP; anticodon-codon recognition; binding of Aa-tRNA; biosynthesis of polypeptides; complementarity; elongation factor Tu; factor-free process; factor-promoted process; free energy; non-complementarity; parallel reactions; proofreading; removal of Aa-tRNA; ribosome

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