Summary
Nucleotide substitutions in the form of transitions (purine-purine or pyrimidine-pyrimidine interchanges) and transversions (purine-pyrimidine interchanges) occur during evolution and may be complied by aligning the sequences of homologous genes. Referring to the genetic code tables, silent transitions take place in third positions of codons in family boxes and two-codon sets. Silent transversions in third positions occur only in family boxes, except for A⇋C transversions between AGR and CGR arginine codons (R=A or G). Comparisons of several protein genes have been made, and various subclasses of transitional and transversional nucleotide substitutions have been compiled. Considerable variations occur among the relative proportions of transitions and transversions. Such variations could possibly be caused by mutator genes, favoring either transitions or, conversely, transversions, during DNA replication. At earlier stages of evolutionary divergence, transitions are usually more frequent, but there are exceptions. No indication was found that transversions usually originate from multiple substitutions in transitions.
Similar content being viewed by others
References
Anderson S, Bankier AT, Barrell BG, de Bruijn MHL, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJH, Staden R, Young IG (1981) Sequence and organization of the human mitochondrial genome. Nature 290:457–465
Anderson S, de Bruijn MHL, Coulson AR, Eperon IC, Sanger F, Young IG (1982) The complete sequence of bovine mitochondrial DNA: conserved features of the mammalian mitochondrial genome. J Mol Biol 155:683–717
Bibb MJ, Van Etten RA, Wright CT, Walberg MW, Clayton DA (1981) Sequence and gene organization of mouse mitochondrial DNA. Cell 26:167–180
Brown GG, Simpson MV (1982) Novel features of animal mtDNA evolution as shown by sequences of two rat cytochrome oxidase subunit II genes. Proc Natl Acad Sci USA 79:3246–3250
Brown WM, Prager EM, Wang A, Wilson AC (1982) Mitochondrial DNA sequences in primates: tempo and mode of evolution. J Mol Evol 18:225–239
Catzeflis FM, Sheldon FH, Ahlquist JH, Sibley C (1987) DNA-DNA hybridization enhancement of the rapid rate of muroidrodent DNA evolution. Mol Biol Evol, vol 4
Clary DO, Wolstenholme DR (1985) The mitochondrial DNA molecule ofDrosophila yakuba: nucleotide sequence, gene organization, and genetic code. J Mol Evol 22:252–271
Clary DO, Wolstenholme DR (1987)Drosophila mitochondrial DNA: conserved sequences in the A+T-rich region and supporting evidence for a secondary structure model of the small ribosomal RNA. J Mol Evol 25:116–125
Connor W, States JC, Mezquita J, Dixon GH (1984) Organization and nucleotide sequence of rainbow trout histone H2A and H3 genes. J Mol Evol 20:236–250
Cox EC, Yanofsky C (1967) Altered base ratios in the DNA of anEscherichia coli mutator strain. Proc Natl Acad Sci USA 58:1895–1902
de Bruijn MHL (1983)Drosophila melanogaster mitochondrial DNA, a novel organization and genetic code. Nature 304: 234–241
DeSalle R, Freedman T, Prager EM, Wilson A (1987) Tempo and mode of sequence evolution in mitochondrial DNA of HawaiianDrosophila. J Mol Evol 26:157–164
Dickerson RE (1971) The structure of cytochromec and the rates of molecular evolution. J Mol Evol 1:26–45
Dickerson RE, Timkovich R (1974) Cytochromesc. In: Boyer PD, Lardy H, Myrbäck K (eds) The enzymes, vol 18. Academic Press, New York, pp 1–280
Edwards v. Aguillard (1985) Brief for amicus curiae. The National Academy of Sciences Urging Affirmance No. 85-1512, US (5th Cir. 1985)
Hawk PB (1907) Practical physiological chemistry. Blakiston, New York
Holmquist R (1983) Transitions and transversions in evolutionary descent: an approach to understanding. J Mol Evol 19:134
Holmquist R, Cantor C, Jukes T (1972) Improved procedures for comparing homologous sequences in molecules of proteins and nucleic acids. J Mol Biol 64:145–161
Ingram VM (1961) Gene evolution and the hemoglobins. Nature 189:704–709
Jukes TH (1982) Silent nucleotide substitions in evolution. Paper presented at the Meeting of the Society for Study of Evolution, Stony Brook NY, June 23, 1982
Jukes TH, Bhushan V (1986) Silent nucleotide substitutions and G+C content of some mitochondrial and bacterial genes. J Mol Evol 24:39–44
Jukes TH, Cantor CR (1969) Evolution of protein molecules. In: Munro HN (ed) Mammalian protein metabolism, vol 3. Academic Press, New York, pp 21–132
Jukes TH, Holmquist R (1972a) Evolutionary clock: nonconstancy of rate in different species. Science 177:530–532
Jukes TH, Holmquist R (1972b) Estimation of evolutionary changes in certain homologous polypeptide chains. J Mol Biol 64:163–179
Kimura M (1980) A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences. J Mol Evol 16:111–120
Li WH, Wu CI, Luo CC (1985) A new method for estimating synonymous and nonsynonymous rates of nucleotide substitution considering the relative likelihood of nucleotide and codon changes. Mol Biol Evol 2:150–174
Limbach KJ, Wu R (1983) Isolation and characterization of two alleles of the chicken cytochromec gene. Nucleic Acids Res 11:8931–8950
Limbach KJ, Wu R (1985a) Characterization of a mouse somatic cytochromec gene and three cytochromec pseudogenes. Nucleic Acids Res 13:617–630
Limbach KJ, Wu R (1985b) Characterization of twoDrosophila melanogaster cytochromec genes and their transcripts. Nucleic Acids Res 13:631–642
Montgomery DL, Leung DW, Smith M, Shalit P, Faye G, Hall BD (1980) Isolation and sequence of the gene for iso-2-cytochromec inSaccharomyces cerevisiae. Proc Natl Acad Sci USA 77:541–545
Nuttall GHF (1904) Blood immunity and blood relationship. Cambridge University Press, London
Ochman H, Wilson AC (1987) A universal substitution rate: evidence from bacteria. J Mol Evol 24:000–000
Ohta T (1973) Slightly deleterious mutant substitutions in evolution. Nature 246:96–98
Perler F, Efstratiadis A, Lomedico P, Gilbert W, Kolodner R, Dogson J (1980) The evolution of genes: the chicken preproinsulin gene. Cell 20:555–566
Reichert ET, Brown AP (1907) Crystallography of hemoglobins from various species. Proc Soc Exp Biol Med 5:66–75
Reichert ET, Brown AP (1909) The differentiation and specificity of corresponding proteins and other vital substances in relation to biological classification and organic evolution: the crystallography of hemoglobins. Carnegie Institution, Washington DC
Sanger F, Thompson EOP, Tuppy H (1952) The structure of insulin. Symposium sur les hormones proteiques and derives des proteins. 2nd Int Congr Biochem. Paris, France, p 26
Scarpulla RC, Agne KM, Wu RJ (1981) Isolation and structure of a rat cytochromec gene. J Biol Chem 256:6480–6486
Schaffner W, Kunz G, Daetwyler H, Telford J, Smith HO, Birnstiel ML (1978) Genes and spacers of cloned sea urchin histone DNA analyzed by sequencing. Cell 14:655–671
Smith M, Leung DW, Gillam S, Astell CR (1979) Sequence of the gene for iso-1-cytochrome c in Saccharomyces cerevisiae. Cell 16:753–761
Speyer J (1965) Mutagenic DNA polymerase. Biochem Biophys Res Commun 21:6–10
Sures I, Lowry J, Kedes L (1978) The DNA sequence of sea urchin (S. purpuratus) H2A, H2B and H3 histone coding and spacer regions. Cell 15:1033–1044
Watson J, Crick FHC (1953) Genetical implications of the structure of deoxyribonucleic acid. Nature 171:964–967
Winkfein RJ, Connor W, Mezquita J, Dixon GH (1985) Histone H4 and H2B genes in rainbow trout (Salmo gairdnerii). J Mol Evol 22:1–19
Zuckerkandl E, Pauling L (1965) Evolutionary divergence and convergence in proteins. In: Bryson V, Vogel HJ (eds) Evolving genes and proteins. Academic Press, New York, pp 97–166
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Jukes, T.H. Transitions, transversions, and the molecular evolutionary clock. J Mol Evol 26, 87–98 (1987). https://doi.org/10.1007/BF02111284
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF02111284