Summary
The evolutionary behavior of two mitochondrial enzymes (L-glycerol 3-phosphate:cytochrome c oxidoreductase E.C.1.1.1.95,αGPO, and L-malate: NAD+ oxidoreductase, E.C.1.1.1.37, m-MDH) obtained from several temperate and tropicalDrosophila species was examined by comparing their catalytic properties, which related to temperature (Km-Ea-Q10-Thermostability). MitochondrialαGPO or m-MDH obtained either from temperate or from tropical species was found to exhibit similar catalytic properties while for both cytosolic enzymes, theαGPDH and s-MDH, Km patterns were similar among species from the same thermal habitat and different between thermal habitats. In combination with other observations reported in the literature these facts support the view that the function, and probably the structure, of mitochondrial enzymes are better conserved in evolution than those of the corresponding enzymes found in the cytosol. It is proposed that the relative invariance of the mitochondrial enzymes structure is probably linked to a necessary relative invariance of molecular interactions inside the mitochondrion.
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References
Alahiotis, S. (1979a). Insect Biochem.9, 189–194
Alahiotis, S. (1979b). Genetika (in press)
Alahiotis, S., Berger, E. (1978). Comp. Biochem. Physiol61B, 199–202
Alahiotis, S., Miller, S., and Berger, E. (1977). Nature (London)269, 144–145
Alahiotis, S., Pelecanos, M. (1978). Can. J. Genet. Cytol.20, 269–273
Cossins, A.A., Prosser, C.L. (1978). Proc. Natl. Acad. Sci (USA)75, 2040–2043
Groot, C.S.P., Rouslin, W., Schatz, G. (1972). J. Biol. Chem.247, 1735–1742
Hall, J., Alahiotis, S., Stzupf, D., White, K. (1980). (Submitted)
Hansford, R.C., Sacktor, B. (1971). In: Chemical zoology, M. Florkin, B.T. Scheer, eds. Vol6, pp. 213–247, New York: Academic Press
Hazel, J.R. (1972). Comp. Biochem. Physiol.43B, 837–861, 863–882
Hochachka, P.W., Somero, G.N. (1973). Strategies of biochemical adaptation. Philadelphia: W.B. Saunders
McReynolds, M., Kitto, B. (1970). Biochim. Biophsy. Acta198, 166–175
Moon, T.W., Hochachka, P.W. (1971). Biochem. J.123, 695–705
Nomura, M., Morgan, E.A., Jaskunas, S.R. (1977). Annu. Rev. Genet.11, 297–348
O'Brien, S.J. (1973). Biochem. Genet.10, 191–205
O'Brien, S.J., Gethman, R.C. (1973). Genetics75, 155–167
O'Brien, S.J., MacIntyre, R.J. (1972). Biochem. Genet.7, 141
Olmsted, J.B., Borisy, G.G. (1973). Nature (London)271, 557–559
Patterson, J.T., Stone W. (1952). Evolution in genusDrosophila. New York: MacMillian
Robert, N., Gray, I. (1972). Comp. Biochem. Physiol.42B, 389–402
Sacktor, B. (1965). In the physiology. In: Insecta M. Rockstein, ed., Vol.2, pp. 483–580. New York: Academic Press
Sacktor, B. (1976). In: Biochem. Soc. Symp. R.M.S. Smellie and J.F. Pennock, eds.41, 111–131. London: The Biochemical Society
Sacktor, B., Dick, A. (1962). J. Biol. Chem.237, 3259–3263
Scislowski, W.D. (1977). Mol. Cell. Biochem.18, 93–99
Sonderegger, P., Christen, P. (1978). Nature (London)275, 157–159
Sonderegger, P., Gehring, J., Christen, P. (1977). J. Biol. Chem.252, 609–612
Tzagoloff, A. (1977). BioScience27, 18–23
Weislogel, P.O. Butow, R.A. (1971). J. Biol. Chem.246, 5113–5119
Woese, C.R. (1977). J. Mol. Evol.10, 93–96
Zebe, E.C., McShan, W.H. (1957). J. Gen. Physiol.40, 779–790
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Alahiotis, S.N. Adaptation ofDrosophila enzymes to temperature. III. Evolutionary conservatism in mitochondrial enzymes. J Mol Evol 16, 37–46 (1980). https://doi.org/10.1007/BF01732068
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DOI: https://doi.org/10.1007/BF01732068