Send to

Choose Destination
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

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Biology Department, Lomonosov Moscow State University, 119192 Moscow, Russia.


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.


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

Supplemental Content

Full text links

Icon for Multidisciplinary Digital Publishing Institute (MDPI) Icon for PubMed Central
Loading ...
Support Center