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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Genetic Code

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Disease relevance of Genetic Code


High impact information on Genetic Code


Chemical compound and disease context of Genetic Code


Biological context of Genetic Code

  • The Curation program contains prior knowledge of the genetic code and of the PAX6 gene including cDNA sequence, location of intron/exon boundaries, and protein domains, so that the minimum of information need be provided by the submitter or Curator [9].
  • These results are best explained by the presence of nonfunctional duplications of a portion of the mtDNA, probably located in the nuclear genome, since transfer into the nuclear gene would render the COI gene nonfunctional due to differences in the nuclear and mitochondrial genetic codes [10].
  • To maintain the correct Watson-Crick base pairing properties of the wobble base (and hence proper translation of the genetic code), TGT must recognize its heterocyclic substrate with high specificity [11].
  • By using the established amino acid sequence of the IF2 H-chain and a knowledge of the genetic code, 14 oligonucleotides were assigned within the constant region and four within the variable region of the IF2 H-chain [12].
  • It uses the "mitochondrial" genetic code, i.e., it contains a TGA codon, whereas all other protein-encoding genes, and all but one intronic open reading frame, use the "standard" genetic code (UGG for tryptophan) [13].

Anatomical context of Genetic Code


Associations of Genetic Code with chemical compounds

  • In this way, CGG codons can be changed to UGG codons in the mRNA so that tryptophan may be encoded according to the universal genetic code [3].
  • RNA helical oligonucleotides that recapitulate the acceptor stems of transfer RNAs, and that are devoid of the anticodon trinucleotides of the genetic code, are aminoacylated by aminoacyl tRNA synthetases [15].
  • In considering evolutionary mechanisms for this curious divergence from the standard genetic code, we propose the existence of progenitor tRNAs for glutamine that can weakly suppress UAA and UAG codons [16].
  • Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code [17].
  • The variations at these two positions and phylogenetic analyses based on the structural information suggest that, in contrast to many other amino acids, discrimination of tyrosine from tryptophan occurred late in the development of the genetic code [18].

Gene context of Genetic Code

  • The universal genetic code is used in both the ND1 and RTL genes; however, the latter is distinguished from the other protein coding genes of C. reinhardtii mtDNA by several characteristics which suggest that RTL may be a more recently acquired gene [19].
  • Mice with the NK1 receptor deleted from their genetic code also have an increased firing rate of 5-HT neurons [20].
  • In human ND2, the amino-terminal methionine is encoded by AUU, which, as in the "universal" genetic code, is also used as an isoleucine codon in elongation [21].
  • The statistical distribution of mutational likelihoods was as predicted on the basis of the PROC cDNA sequence alone, allowing however for the redundancy of the genetic code [22].
  • AARS catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid [23].

Analytical, diagnostic and therapeutic context of Genetic Code


  1. Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion. Kobayashi, T., Sakamoto, K., Takimura, T., Sekine, R., Kelly, V.P., Vincent, K., Kamata, K., Nishimura, S., Yokoyama, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  2. Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus. Manfredi, G., Fu, J., Ojaimi, J., Sadlock, J.E., Kwong, J.Q., Guy, J., Schon, E.A. Nat. Genet. (2002) [Pubmed]
  3. RNA editing in wheat mitochondria results in the conservation of protein sequences. Gualberto, J.M., Lamattina, L., Bonnard, G., Weil, J.H., Grienenberger, J.M. Nature (1989) [Pubmed]
  4. A specific amino acid binding site composed of RNA. Yarus, M. Science (1988) [Pubmed]
  5. Amino acid composition of proteins: Selection against the genetic code. Jukes, T.H., Holmquist, R., Moise, H. Science (1975) [Pubmed]
  6. Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition. Swairjo, M.A., Otero, F.J., Yang, X.L., Lovato, M.A., Skene, R.J., McRee, D.E., Ribas de Pouplana, L., Schimmel, P. Mol. Cell (2004) [Pubmed]
  7. Reassigning cysteine in the genetic code of Escherichia coli. Döring, V., Marlière, P. Genetics (1998) [Pubmed]
  8. Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo. Blight, S.K., Larue, R.C., Mahapatra, A., Longstaff, D.G., Chang, E., Zhao, G., Kang, P.T., Green-Church, K.B., Chan, M.K., Krzycki, J.A. Nature (2004) [Pubmed]
  9. The Human PAX6 Mutation Database. Brown, A., McKie, M., van Heyningen, V., Prosser, J. Nucleic Acids Res. (1998) [Pubmed]
  10. Mitochondrial pseudogenes are pervasive and often insidious in the snapping shrimp genus Alpheus. Williams, S.T., Knowlton, N. Mol. Biol. Evol. (2001) [Pubmed]
  11. Role of aspartate 143 in Escherichia coli tRNA-guanine transglycosylase: alteration of heterocyclic substrate specificity. Todorov, K.A., Garcia, G.A. Biochemistry (2006) [Pubmed]
  12. Purification and sequence analysis of the mRNA coding for an immunoglobulin heavy chain. Cowan, N.J., Secher, D.S., Milstein, C. Eur. J. Biochem. (1976) [Pubmed]
  13. Characterization of a novel open reading frame, urf a, in the mitochondrial genome of fission yeast: correlation of urf a mutations with a mitochondrial mutator phenotype and a possible role of frameshifting in urf a expression. Zimmer, M., Krabusch, M., Wolf, K. Curr. Genet. (1991) [Pubmed]
  14. In vitro suppression of UGA codons in a mitochondrial mRNA. De Ronde, A., Van Loon, A.P., Grivell, L.A., Kohli, J. Nature (1980) [Pubmed]
  15. An operational RNA code for amino acids and possible relationship to genetic code. Schimmel, P., Giegé, R., Moras, D., Yokoyama, S. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  16. Physiological levels of normal tRNA(CAGGln) can effect partial suppression of amber mutations in the yeast Saccharomyces cerevisiae. Weiss, W.A., Edelman, I., Culbertson, M.R., Friedberg, E.C. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  17. Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code. Jester, B.C., Levengood, J.D., Roy, H., Ibba, M., Devine, K.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  18. Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Yang, X.L., Otero, F.J., Skene, R.J., McRee, D.E., Schimmel, P., Ribas de Pouplana, L. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  19. Genes encoding a subunit of respiratory NADH dehydrogenase (ND1) and a reverse transcriptase-like protein (RTL) are linked to ribosomal RNA gene pieces in Chlamydomonas reinhardtii mitochondrial DNA. Boer, P.H., Gray, M.W. EMBO J. (1988) [Pubmed]
  20. Impact of substance P receptor antagonism on the serotonin and norepinephrine systems: relevance to the antidepressant/anxiolytic response. Blier, P., Gobbi, G., Haddjeri, N., Santarelli, L., Mathew, G., Hen, R. Journal of psychiatry & neuroscience : JPN. (2004) [Pubmed]
  21. Initiation codons in mammalian mitochondria: differences in genetic code in the organelle. Fearnley, I.M., Walker, J.E. Biochemistry (1987) [Pubmed]
  22. The mutational demography of protein C deficiency. Krawczak, M., Reitsma, P.H., Cooper, D.N. Hum. Genet. (1995) [Pubmed]
  23. The new aspects of aminoacyl-tRNA synthetases. Szymański, M., Deniziak, M., Barciszewski, J. Acta Biochim. Pol. (2000) [Pubmed]
  24. Probing the role of tryptophans in Aequorea victoria green fluorescent proteins with an expanded genetic code. Budisa, N., Pal, P.P., Alefelder, S., Birle, P., Krywcun, T., Rubini, M., Wenger, W., Bae, J.H., Steiner, T. Biol. Chem. (2004) [Pubmed]
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