Abstract

The genetic code is said to be redundant in that the same amino acid residue can be encoded by multiple, so-called synonymous, codons. If all properties of synonymous codons were entirely equivalent, one would expect that they would be equally distributed along protein coding sequences. However, many studies over the last three decades have demonstrated that their distribution is not entirely random. It has been postulated that certain codons may be translated by the ribosome faster than others and thus their non-random distribution dictates how fast the ribosome moves along particular segments of the mRNA. The reasons behind such segmental variability in the rates of protein synthesis, and thus polypeptide emergence from the ribosome, have been explored by theoretical and experimental approaches. Predictions of the relative rates at which particular codons are translated and their impact on the nascent chain have not arrived at unequivocal conclusions. This is probably due, at least in part, to variation in the basis for classification of codons as “fast” or “slow”, as well as variability in the number and types of genes and proteins analyzed. Recent methodological advances have allowed nucleotide-resolution studies of ribosome residency times in entire transcriptomes, which confirm the non-uniform movement of ribosomes along mRNAs and shed light on the actual determinants of rate control. Moreover, experiments have begun to emerge that systematically examine the influence of variations in ribosomal movement and the fate of the emerging polypeptide chain.

Highlights

  • The genetic code is said to be redundant in that the same amino acid residue can be encoded by multiple, so-called synonymous, codons

  • The template is composed of a specific combination of 61 stringent in the first two nucleotide positions of the minihelix than in trinucleotide codons which encode 20 amino acids

  • Codons are read by adaptor molecules called transfer RNA post-transcriptional deamination of adenosine to that bear matching trinucleotide sequences, or anticodons. inosine in the first anticodon position (INN) expands the decoding

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Summary

Protein synthesis and the redundancy of the genetic code

The transfer of genetic information into protein products is bonds [4]. Interestingly, there are three conserved nucleotides in the termed translation (Figure 1; for detailed reviews on the mechanisms bacterial 70S ribosome which maintain decoding fidelity by of translation, please see [1,2,3]). Inosine in the first anticodon position (INN) expands the decoding This reading or decoding of the codon occurs by recognition through capacity from strictly Watson-Crick (A:U) to other allowed base pairing, where at least two hydrogen bonds are formed between “wobble” base pairing (I:U, I:C, I:A) [4]. Nucleotide of the anticodon, the so-called Wobble position, Upon decoding, peptide bond formation is catalyzed in the peptidylnonstandard base pairing can occur and results in altered base stacking transferase center of the ribosome and is followed by translocation of conformations that are different from that of Watson-Crick pairing the ribosome to the codon.

Polypeptide elongation rate determinants
Genetic Code Redundancy
Polypeptide elongation rates and protein folding
Full Text
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