Abstract
If genome space is finite with little, if any, DNA that is not functional under some circumstance, then potential conflicts between different forms of genomic information must be resolved by appropriate trade-offs. These trade-offs sometimes require that genes accommodate spacers, introns, and simple sequence elements. The nature and extent of the trade-offs varies with the biological species. Study of trade-offs is facilitated in genes or species where demands are exceptional (e.g. genes under positive selection pressure to adapt proteins, genes that overlap, and species under extreme downward or upward GC-pressures). Spacers and introns are likely to have existed early in evolution because they are preferential sites for the stem-loop structures that are necessary for initiating recombination and, hence, error-detection and correction. Genes, as recognized today, would have arisen in sequences already adapted for these purposes. Purine-loading pressure would have supported protein-pressure in provoking the splitting into introns of what might otherwise have been large exons. From this perspective we can understand why the genes of the malaria parasite are extraordinarily long, and we can identify the potential Achilles heel of the AIDS virus as the dimer-linkage sequence that is essential for the copackaging of disparate genomes, so allowing recombination repair in a future host.
Ideas in the theory of evolution can be used in situations far removed from biology. Similarly, information theory has ideas that are widely applicable to situations remote from its original inspiration.
Richard Hamming (1980) [1]
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References
Hamming RW (1980) Coding and Information Theory. Prentice-Hall, Englewood Cliffs
Booth A, Doolittle WF (2015) Eukaryogenesis, how special really? Proceedings of the National Academy of Sciences USA 112:10278–10285
Federoff NV (1979) On spacers. Cell 16:687–710
Scherrer K (2003) The discovery of ‘giant’ RNA and RNA processing. Trends in Biochemical Sciences 28:566–571
Gilbert W (1978) Why genes in pieces? Nature 271:501
Weber K, Kabsch W (1994) Intron positions in actin genes seem unrelated to the secondary structure of the protein. EMBO Journal 13:1280–1288
Stoltzfus A, Spencer DF, Zuker M, Logsdon JM, Doolittle WF (1994) Testing the exon theory of genes: evidence from protein structure. Science 265:202–207
Sakharkar M, Passetti F, Souza JE de, Long M, Souza SJ de (2002) ExInt: an Exon Intron Database. Nucleic Acids Research 30:191–194
Blake C (1983) Exons – present from the beginning. Nature 306:535–537
Naora H, Deacon NJ (1982) Relationship between the total size of exons and introns in protein-coding genes of higher eukaryotes. Proceedings of the National Academy of Sciences USA 79:6196–6200
Raible F, et al. (2005) Vertebrate-type intron-rich genes in the marine annelid Platynereis dumerilii. Science 310:1325–1326
Liu M, Grigoriev A (2004) Protein domains correlate strongly with exons in multiple eukaryotic genomes – evidence of exon shuffling? Trends in Genetics 20:399–403
Forsdyke DR (1981) Are introns in-series error-detecting codes? Journal of Theoretical Biology 93:861–866
Reanney DC (1987) Genetic error and genome design. Cold Spring Harbor Symposium on Quantitative Biology 52:751–757
Forsdyke DR (2013) Introns first. Biological Theory 7:196–203
Bernstein C, Bernstein H (1991) Aging, Sex and DNA Repair. Academic Press, San Diego
Williams GC (1966) Adaptation and Natural Selection. A Critique of Some Current Evolutionary Thought. Princeton University Press, Princeton, pp 133–138 [Because RNA can play both templating and structural roles, it is an attractive candidate for being ‘the primordial life molecule.’ Hence we speak of an early “RNA world.” Information storage and templating (its digital roles) would have later devolved to DNA (with mRNA acting as a short-lived intermediate), and many structure-dependent functions (its analog roles) would have devolved to proteins. Nevertheless, in various forms RNA retains its flexibility today.]
Forsdyke DR (1995). A stem-loop ‘kissing’ model for the initiation of recombination and the origin of introns. Molecular Biology & Evolution 12:949–958
Forsdyke DR (1995) Conservation of stem-loop potential in introns of snake venom phospholipase A2 genes. An application of FORS-D analysis. Molecular Biology & Evolution 12:1157–1165
Leicht BG, Muse SV, Hanczyc M, Clark AG (1995) Constraints on intron evolution in the gene encoding the myosin alkali light chain in Drosophila. Genetics 139:299–308
Forsdyke DR. (1996) Stem-loop potential: a new way of evaluating positive Darwinian selection? Immunogenetics 43:182–189
Forsdyke DR (1995) Reciprocal relationship between stem-loop potential and substitution density in retroviral quasispecies under positive Darwinian selection. Journal of Molecular Evolution 41:1022–1037
Zhang C-Y, Wei J-F, He S-H (2005) The key role for local base order in the generation of multiple forms of China HIV-1 B/C intersubtype recombinants. BMC Evolutionary Biology 5:53
Alvarez-Valin F, Tort JF, Bernardi G (2000) Nonrandom spatial distribution of synonymous substitutions in the GP63 gene from Leishmania. Genetics 155:1683–1692
Bustamente CD, Townsend JP, Hartl DL (2000) Solvent accessibility and purifying selection within proteins of Escherichia coli and Salmonella enterica. Molecular Biology & Evolution 17:301–308
Heximer SP, Cristillo AD, Russell L, Forsdyke DR (1996) Sequence analysis and expression in cultured lymphocytes of the human FOSB gene (G0S3). DNA Cell Biology 12:1025–1038
Forsdyke DR (1991) Programmed activation of T-lymphocytes. A theoretical basis for short term treatment of AIDS with azidothymidine. Medical Hypothesis 34:24–27 [The HIV hypermutation strategy to ‘outwit’ our adaptive immune defenses makes a mockery of attempts to vaccinate.]
Williams SA, et al. (2005) Prostratin antagonizes HIV latency by activating NF-kappaB. Journal of Biological Chemistry 279:42008–42017 [HIV may have an Achilles heel, but first latent HIV must be ‘flushed’ from the genome using “inductive therapy.”]
Shetty S, Kim S, Shimakami T, Lemon SM, Mihailescu M-R (2010) Hepatitis C virus genomic RNA dimerization is mediated via a kissing complex intermediate. RNA 16:913–925
Kurahashi H, Inagaki H, Yamada K, Ohye T, Taniguchi M, Emanuel BS, Toda T (2004) Cruciform DNA structure underlies the etiology for palindrome-mediated human chromosomal translocations. Journal of Biological Chemistry 279:35377–35383
Lu S, Wang G, Bacolla A, Zhao J, Spitser S, Vasquez KM (2015) Short inverted repeats are hotspots for genetic instability: relevance to cancer genomes. Cell Reports 10:1674–1680
Thanaraj TA, Argos P (1996) Protein secondary structural types are differentially coded in messenger RNA. Protein Science 5:1973–1983
Lang DM (2005) Imperfect DNA mirror repeats in E. coli TnsA and other protein-coding DNA. Biosystems 81:183–207
Barrette IH, McKenna S, Taylor DR, Forsdyke DR (2001) Introns resolve the conflict between base order-dependent stem-loop potential and the encoding of RNA or protein. Further evidence from overlapping genes. Gene 270:181–189
Grantham R (1974) Amino acid difference formula to help explain protein evolution. Science 185:862–864 [To construct a “PAM matrix,” the observed frequency of interchanges between two amino acids is divided by the expected interchanges calculated by multiplying the respective frequencies of each amino acid in the data set. There being 20 amino acids, a 20 × 20 matrix is generated. Of the 400 values, 20 are on the diagonal and the remaining 380 are duplicates, so that 190 values form the final matrix. Two proteins whose amino acid differences generate a low total PAM score would be held to be closely related evolutionarily.]
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Forsdyke, D.R. (2016). Exons and Introns. In: Evolutionary Bioinformatics. Springer, Cham. https://doi.org/10.1007/978-3-319-28755-3_13
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DOI: https://doi.org/10.1007/978-3-319-28755-3_13
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