That scheme is often referred to as the canonical or standard genetic code, or simply the genetic code, though variant codes (such as in mitochondria) exist. While the "genetic code" is what determines a protein's amino acid sequence, other genomic regions determine when and where these proteins are produced according to various "gene regulatory codes". == History == Efforts to understand how proteins are encoded began after DNA's structure was discovered in 1953.
This work was based upon Ochoa's earlier studies, yielding the latter the Nobel Prize in Physiology or Medicine in 1959 for work on the enzymology of RNA synthesis. Extending this work, Nirenberg and Philip Leder revealed the code's triplet nature and deciphered its codons.
Matthaei were the first to reveal the nature of a codon in 1961. They used a cell-free system to translate a poly-uracil RNA sequence (i.e., UUUUU...) and discovered that the polypeptide that they had synthesized consisted of only the amino acid phenylalanine.
Khorana, Holley and Nirenberg received the 1968 Nobel for their work. The three stop codons were named by discoverers Richard Epstein and Charles Steinberg.
Even models are proposed that predict "entry points" for synthetic amino acid invasion of the genetic code. Since 2001, 40 non-natural amino acids have been added into protein by creating a unique codon (recoding) and a corresponding transfer-RNA:aminoacyl – tRNA-synthetase pair to encode it with diverse physicochemical and biological properties in order to be used as a tool to exploring protein structure and function or to create novel or enhanced proteins. H.
Benner constructed a functional 65th (in vivo) codon. In 2015 N.
Söll and co-workers reported the full substitution of all 20,899 tryptophan residues (UGG codons) with unnatural thienopyrrole-alanine in the genetic code of the bacterium Escherichia coli. In 2016 the first stable semisynthetic organism was created.
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