Full text in pdf format

 

Malate dehydrogenase polymorphism in Amazon Curimatids (Teleostei: Curimatidae) : Evidence of an ancient mutational event

 

 

Mércia Cristina de Magalhães Caraciolo; Adalberto Luis Val; Vera Maria Fonseca de Almeida-Val

AQUACULTURA - Instituto Nacional de Pesquisas da Amazônia (INPA), Ministério de Ciência e Tecnologia, Alameda Cosme Ferreira 1756, Caixa Postal 478, 69083-000 Manaus, AM, Brasil. Send correspondence to V.M.F.A.-V.

 

 


ABSTRACT

Electrophoretic mobilities and tissue expression of MDH (malate dehydrogenase) were found to be the same for 12 Curimatidae fish species from the Amazon basin. Similarities in the migration of isozymes produced by sMDH-A* and sMDH-B* allowed no differentiation among these species. Out of 12, six species showed two alleles for sMDH-B*. These alleles, named sMDH-B*100 and sMDH-B*85, were present at different frequencies among the six species. B85 and/or B100/85 phenotypes were generally more thermostable than B100 phenotypes. Based on the occurrence of a single allele (B*85) in six different species, their different frequencies, and their heat inactivation rates, the following hypotheses are suggested: a) the alleles are the result of a single mutational event occurring before the speciation process in this family, orb) they are cryptic alleles, a result of different mutational events.

Keywords: malate dehydrogenase; polymorphism; Amazon Curimatids; ancient mutational event.


 

 

REFERENCES

Aspinwall, N. (1974). Genetic analysis of duplicate malate dehydrogenase loci in the pink salmon, Oncorhynchus gorbuscha. Genetics 76: 65-72.

Ayala, F.J. (1982). Molecular polymorphism: How much is there and why is there so much? Devel. Genet. 4: 379-391.

Bailey, G.S., Cocks, G.T. and Wilson, A.C. (1969). Gene duplication in fishes: malate dehydrogenase of salmon and trout. Biochem. Biophys. Res. Comm. 34: 605-612.

Bailey, G.S., Wilson, A.C., Halver, J.E. and Johnson, C.L. (1970). Multiple forms of supernatant malate dehydrogenase in salmonid fishes: biochemical, immunological and genetic studies. J. Biol. Chem. 245: 5927-5940.

Basaglia, F. (1991). Malate dehydrogenase isozymes in fifteen sparidae species (Perciformes, Teleostei). Comp. Biochem. Physiol. 98B: 9-19.

Buth, D.G. (1983). Duplicate isozyme loci in fishes: Origins, distribution, phyletic consequences and locus nomenclature. In: Isozymes: Current Topics in Biological and Medical Research. (Rattazzi, M.C., Scandalios, J.G. and Whitt, G.S., eds.). Vol. 10. Alan R. Liss, New York, pp. 381-400.

Buth, D.G. (1984). The application of electrophoretic data in systematic studies. Ann. Rev. Ecol. Syst. 15: 501-522.

Coppes, Z.L., Schwantes, M.L.B. and Schwantes, A.R. (1987). Adaptative features of enzymes from the family Scianidae (Perciformes) - I. Studies of soluble malate dehydrogenase (s-MDH) and creatine kinase (CK) of fishes from the south coast of Uruguai. Comp. Biochem. Physiol. 88B: 203-209.

Coyne, J.A., Felton, A.A. and Lewontin, R.C. (1978). Extent of genetic variation at a highly polymorphic esterase locus in Drosophila pseudobscura. Proc. Natl. Acad. Sci. USA 75: 5090-5093.

De Luca, P.H., Schwantes, M.L.B. and Schwantes, A.R. (1983). Adaptative features of ectothermic enzymes. IV. Studies on malate dehydrogenase of Astyanax fasciatus (Characidae) from Lobo reservoir (São Carlos, São Paulo, Brasil). Comp. Biochem. Physiol. 74B: 315-324.

Fenerich-Verani, N., Schwantes, M.L.B. and Schwantes, A.R. (1990). Patterns of gene expression during Prochilodus scrofa (Characiformes, Prochilodontidae) embryogenesis. I. Lactate dehydrogenase. Comp. Biochem. Physiol. 97B: 235-246.

Ferris, S.D. (1984). Tetraploidy and the evolution of the catostomid fishes. In: Evolutionary Genetics of Fish (Turner, B.J., ed.). Plenum Publishing Corp., New York, pp. 55-93.

Fisher, S.E., Shaklee, J.B., Ferris, S.D. and Whitt, G.S. (1980). Evolution of five multilocus isozyme systems in the chordates. In: Animal Genetics and Evolution (Vorontsov, N.N. and von Brink, J.M., eds.). vol. 52: 73-85.

Hedrick, P.W. (1983). Genetics of Population (Lipsett, S., ed.). Science Books International, Boston, pp. 629.

Hines, S.A., Philipp, D.P., Childers, W.F. and Whitt, G.S. (1983). Thermal kinetic differences between allelic isozymes of malate dehydrogenase (MDH-B) of largemouth bass, Micropterus salmonoides. Biochem. Genet. 21: 1143-1151.

Hochachka, P.W. (1967). Organization of metabolism during temperature compensation. In: Molecular Aspects of Temperature Adaptation. (Prosser, C.L., ed.). American Association for the Advancement of Science Symposium Series, 84: 177-203, Washington D.C.

Hochachka, P.W. and Somero, G.N. (1984). Biochemical Adaptation. Princeton Univ. Press, Princeton, pp. 537.

Kreitzman, H. (1983). Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster. Nature 304: 412-417.

Lewontin, R.C. (1985). Population genetics. In: Evolution. (Greenwood, P.J., Harvey, P.H. and Slatkin, M., eds.). Cambridge University Press, Cambridge, pp. 3-18.

Meizel, S. and Markert, C.L. (1967). Malate dehydrogenase isozymes of the marine snail, Ieyanasse obsoluta. Arch. Biochem. Biophy. 127: 753-765.

Ohno, S. (1970). The enormous diversity in genome sizes of fish as a reflection of nature's extensive experiments with gene duplication. Trans. Amer. Fish. Soc. 99: 120-130.

Place, A.R. and Powers, D.A. (1978). Genetic bases for protein polymorphism in Fundulus heteroclitus (L.). I. Lactate dehydrogenase (Ldh-B), malate dehydrogenase (Mdh-B), glucosephosphate isomerase (Gpi-B), and phosphoglucomutase (Pgm-A). Biochem. Genet. 16: 577-591.

Rainboth, W.J. and Whitt, G.S. (1974). Analysis of evolutionary relationships among shiners of the subgenus Luxilus (Teleostei, Cypriniformes, Notropis) with the lactate dehydrogenase and malate dehydrogenase isozyme systems. Comp. Biochem. Physiol. 49B: 241-252.

Schwantes, M.L.B. and Schwantes, A.R. (1982a). Adaptative features of ectothermic enzymes - I. Temperature effects on the malate dehydrogenase from a temperate fish Leiostomus xanthurus. Comp. Biochem. Physiol. 72B: 49-58.

Schwantes, M.L.B. and Schwantes, A.R. (1982b). Adaptative features of the ectothermic enzymes - II. The effects of acclimation temperature on the malate dehydrogenase of the spot, Leiostomus xanthurus. Comp. Biochem. Physiol. 72B: 59-64.

Sechs, L. (1982). Applied Statistics: a Handbook of Techniques. Springer Verlag, New York, pp. 299-306.

Shaklee, J.B., Allendorf, F.W., Morizot, D.C. and Whitt, G.S. (1989). Genetic nomenclature for proteins-coding loci in fish: Proposed guidelines. Trans. Amer. Fish. Soc. 118: 218-277.

Shaw, R.R. and Prassad, R. (1970). Starch gel electrophoresis of enzymes. A compilation of recipes. Biochem. Genet. 4: 297-320.

Singh, R.S., Lewontin, R.C. and Felton, A.A. (1976). Genetic heterogeneity within electrophoretic "alleles" of xanthine dehydrogenase in Drosophila pseudobscura. Genetics 84: 609-629.

Smithies, 0. (1955). Zone electrophoresis in starch gel: group variation in the serum protein of normal human adults. J. Biochem. 61: 629-641.

Smithies, 0. (1959). An improved procedure for starch gel electrophoresis: further variation in the serum proteins of normal individuals. J. Biochem. 71: 585-587.

Somero, G.N. and Hochachka, P.W. (1969). Isoenzymes and short-term temperature compensation in poikilotherms: activation of lactate dehydrogenase isoenzyme by temperature decreases. Nature 223: 194-195.

Tsukuda, H. (1975). Temperature of the relative activities of liver lactate dehydrogenase isozymes in goldfish acclimated to different temperatures. Comp. Biochem. Physiol. 52B: 343-345.

Val, A.L., Schwantes, A.R., Schwantes, M.L.B. and De Luca, P.H. (1981). Amido hidrolisado do milho como suporte eletroforético. Ciênc. Cult. 33: 992-996.

Vari, R.P. (1988). The Curimatidae, a lowland neotropical family (Pisces: Characiformes): distribution, endemism and phylogenetic biogeography. In: Proceedings of a Workshop on Neotropical Distribution Patterns. Academia Brasileira de Ciências, Rio de Janeiro, pp. 343-377.

Wheat, T.E., Childers, W.F., Miller, E.T. and Whitt, G.S. (1971). Genetic and in vitro molecular hybridization of malate dehydrogenase isozyme in an interspecific bass (Micropterus) hybrid. Anim. Blood. Grp. Biochem. Genet. 2: 3-14.

Whitt, G.S. (1970). Developmental genetics of the lactate dehydrogenase isozymes of fish. J. Exp. Zool. 175: 1-3.

Whitt, G.S. (1983). Isozymes as probes and participants in developmental and evolutionary genetics. In: Isozymes: Genetics and Evolution. (Rattazzi, M.C., Scandalios, J.G. and Whitt, G.S., eds.). Alan R. Liss Inc., New York, pp. 1-40.

Whitt, G.S. (1987). Species differences in isozyme tissue patterns: their utility for systematic and evolutionary analysis. In: Isozymes: Current Topics in Biological and Medical Research. (Rattazzi, G.C.; Scandalios, J.G. and Whitt, G.S., eds.). Alan Liss Inc., New York, pp. 1-26.

Whitt, G.S., Miller, E.T. and Shaklee, J.B. (1973). Developmental and biochemical genetics of the lactate dehydrogenase isozymes in fishes. In: Genetics and Mutagenesis of Fish. (Schroder, J.H., ed.). Springer-Verlag, Berlin, pp. 243-276.

Yamawaki, H. and Tsukuda, H. (1979a). Significance of the variation in isozymes of liver lactate dehydrogenase with thermal acclimation in goldfish. I. Thermostability temperature dependence. Comp. Biochem. Physiol. 62B: 89-93.

Yamawaki, H. and Tsukuda, H. (1979b). Significance of the variation in isozymes of liver lactate dehydrogenase with thermal acclimation in goldfish. II. Effect of pH. Comp. Biochem. Physiol. 62B: 94-95.

Zink, M.W. and Shaw, D.A. (1968). Regulation of malic enzyme and malic dehydrogenase in Neurospora crassa. Canad. J. Microbiol. 14: 907-912.