×

A novel Lie algebra of the genetic code over the Galois field of four DNA bases. (English) Zbl 1100.92021

Summary: Starting from the four DNA bases order in the Boolean lattice, a novel Lie Algebra of the genetic code is proposed. Here, the main partitions of the genetic code table were obtained as equivalence classes of quotient spaces of the genetic code vector space over the Galois field of the four DNA bases. The new algebraic structure shows strong connections among algebraic relationships, codon assignments and physicochemical properties of amino acids. Moreover, a distance defined between codons expresses a physicochemical meaning. It was also noticed that the distance between wild type and mutant codons tends to be small in mutational variants of four genes: human phenylalanine hydroxylase, human \(\beta\)-globin, HIV-1 protease and HIV-1 reverse transcriptase. These results strongly suggest that deterministic rules in genetic code origin must be involved.

MSC:

92C40 Biochemistry, molecular biology
17D92 Genetic algebras
17B99 Lie algebras and Lie superalgebras

References:

[1] Bashford, J. D.; Jarvis, P. D., The genetic code as a periodic table, Biosystems, 57, 147 (2000)
[2] Bashford, J. D.; Tsohantjis, I.; Jarvis, P. D., A supersymmetric model for the evolution of the genetic code, Proc. Natl. Acad. Sci. USA, 95, 987 (1998)
[3] Beland, P.; Allen, T. F., The origin and evolution of the genetic code, J. Theor. Biol., 170, 359 (1994)
[4] Birkhoff, G.; MacLane, S., A survey of Modern Algebra (1941), The Macmillan Company: The Macmillan Company New York · Zbl 0061.04802
[5] Chothia, C. H., Hydrophobic bonding and accessible surface area in proteins, Nature, 248, 338 (1974)
[6] Chothia, C. H., Structural invariants in protein folding, Nature, 354, 304 (1975)
[7] Crick, F. H.C., The origin of the genetic code, J. Mol. Biol., 38, 367 (1968)
[8] Eck, R. V., Genetic code – emergence of a symmetrical pattern, Science, 140, 477 (1963)
[9] Epstein, C. J., Role of the amino-acid “code” and of selection for conformation in the evolution of proteins, Nature, 210, 25 (1966)
[10] Fauchere, J. L.; Pliska, V., Hydrophobic parameters pi of amino acid side chains from the partitioning of \(N\)-acetyl-amino-acid amides, Eur. J. Med. Chem., 18, 369 (1983)
[11] Geer, L. Y.; Domrachev, M.; Lipman, D. J.; Bryant, S. H., CDART: protein homology by domain architecture, Genome Res., 10, 1619 (2002)
[12] Gillis, D.; Massar, S.; Cerf, N. J.; Rooman, M., Optimality of the genetic code with respect to protein stability and amino acid frequencies, Genome Biol., 2 (2001), (research0049.1-research0049.12)
[13] Grantham, R., Amino acid difference formula to help explain protein evolution, Science, 185, 862 (1974)
[14] Hornos, J. E.; Hornos, Y. M., Algebraic model for the evolution of the genetic code, Phys. Rev. Lett., 71, 4401 (1993)
[15] Jiménez-Montaño, M. A., The hypercube structure of the genetic code explains conservative and non-conservative amino acid substitutions in vivo and in vitro, Biosystems, 39, 117 (1996)
[16] Jukes, T. H., The amino acid code, (Neuberger, A., Comprehensive Biochemistry (1977), Elsevier: Elsevier Amsterdam), 235
[17] Kostrikin, A. I., Introducción al algebra (1980), Editorial MIR: Editorial MIR Moscú · Zbl 0467.01017
[18] Lehmann, J., Physico-chemical constraints connected with the coding properties of the genetic system, J. Theor. Biol., 202, 129 (2000)
[19] Marchler-Bauer, A.; Bryant, S. H., CD-Search: protein domain annotations on the fly, Nucl. Acids Res., 32, W327 (2004)
[20] Miyazawa, S.; Jernigan, R. L., Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation, Macromolecules, 18, 534 (1985)
[21] Miyazawa, S.; Jernigan, R. L., Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading, J. Mol. Biol., 256, 623 (1996)
[22] L.S. Pontriaguin, Grupos Continuos, Editorial Mir, Moscow, Capı´tulo 10, 1978, p. 338.; L.S. Pontriaguin, Grupos Continuos, Editorial Mir, Moscow, Capı´tulo 10, 1978, p. 338.
[23] Redéi, L., Algebra, vol. 1 (1967), Akadémiai Kiadó: Akadémiai Kiadó Budapest · Zbl 0191.00502
[24] Robin, D.; Knight, R. D.; Freeland, S. J.; Landweber, L. F., Selection, history and chemistry: the three faces of the genetic code, Trends Biochem. Sci., 24, 241 (1999)
[25] Rose, G. D.; Geselowitz, A. R.; Lesser, G. J.; Lee, R. H.; Zehfus, M. H., Hydrophobicity of amino acid residues in globular proteins, Sciences, 229, 834 (1985)
[26] Sánchez, R.; Grau, R.; Morgado, E., Genetic code Boolean algebras, WSEAS Trans. Biol. Biomed., 1, 190 (2004)
[27] Sánchez, R.; Grau, R.; Morgado, E., The genetic code Boolean lattice, MATCH Commun. Math. Comput. Chem, 52, 29 (2004) · Zbl 1079.92053
[28] Sánchez, R.; Morgado, E.; Grau, R., A genetic code Boolean structure I. The meaning of Boolean deductions, Bull. Math. Biol., 67, 1 (2005) · Zbl 1334.92317
[29] Sánchez, R.; Perfetti, L. A.; Grau, R.; Morgado, E., A New DNA sequences vector space on a genetic code Galois field, MATCH Commun. Math. Comput. Chem., 54, 3 (2005) · Zbl 1270.92017
[30] Siemion, I. Z.; Siemion, P. J.; Krajewski, K., Chou-Fasman conformational amino acid parameters and the genetic code, Biosystems, 36, 231 (1995)
[31] M.V. Volkenshtein, Biofı´sica. Editorial MIR, Moscú, Capı´tulo 17, 1985, p. 621.; M.V. Volkenshtein, Biofı´sica. Editorial MIR, Moscú, Capı´tulo 17, 1985, p. 621.
[32] Woese, C. R., Order in the genetic code, Proc. Natl. Acad. Sci. USA, 54, 71 (1965)
[33] Yang, Z., Adaptive molecular evolution, (Balding, M.; Bishop, M.; Cannings, C., Handbook of Statistical Genetics (2000), Wiley: Wiley London), 327
This reference list is based on information provided by the publisher or from digital mathematics libraries. Its items are heuristically matched to zbMATH identifiers and may contain data conversion errors. In some cases that data have been complemented/enhanced by data from zbMATH Open. This attempts to reflect the references listed in the original paper as accurately as possible without claiming completeness or a perfect matching.