Summary
The post-translational addition of tyrosine toa-tubulin, catalyzed by tubulin:tyrosine ligase, has been previously reported in mammals and birds. The present study demonstrated that significant ligase activity was present in representative organisms from several other major vertebrate classes (chondrichthyes through reptiles) and that both substrate and enzyme from all vertebrates investigated were compatible with mammalian ligase and tubulin in the tyrosination reaction. None of the invertebrate tissues examined showed incorporation of tyrosine, phenylalanine or dihydroxyphenylalanine intoa tubulin under conditions allowing significant incorporation of these compounds in vertebrate supernatant samples. The failure of invertebrate tubulin to incorporate tyrosine in vitro did not appear to be due to saturation of the carboxyl terminal position with tyrosine or the presence of a soluble inhibitor of ligase activity.
Although tubulin amino acid composition has been highly conserved throughout evolution, a major evolutionary divergence is described based upon biochemical differences whereby invertebrate tubulin cannot be tyrosinated or posttranslationally modified with phenylalanine or dihydroxyphenylalanine under conditions suitable for the incorporation of these compounds by vertebratea tubulin.
Similar content being viewed by others
References
Arce, C.A., Barra, H.S., Rodriguez, J.A., Caputto, R. (1975). FEBS Lett.50, 5–7
Arce, C.A., Hallak, M.E., Rodriguez, J.A., Barra, H.S., Caputto, R. (1978). J. Neurochem.31, 205–210
Argaraña, C.E., Arce, C.A., Barra, H.S., Caputto, R. (1977). Arch. Biochem. Biophys.180, 264–268
Barnes, R.D. (1974). Invertebrate Zoology, 3rd Edition, Philadelphia: W.B. Saunders Co.
Barra, H.S., Rodriguez, J.A., Arce, C.A., Caputto, R. (1973). J. Neurochem.20, 97–108
Deanin, G.G., Gordon, M.W. (1976). Biochem. Biophys. Res. Commun.60, 1384–1390
Deanin, G.G., Thompson, W.C., Gordon, M.W. (1977). Dev. Biol.57, 230–233
Gozes, I., Littauer, U.Z. (1978). Nature276, 411–413
Hildemann, W.H. (1974). Life Sci.14, 605–614
Kobayashi, Y., Mohri, H. (1977). J. Mol. Biol.116, 613–617
Kobayashi, T., Flavin, M. (1978). J. Cell Biol.79, Abstract No. 1825
Laemmli, U.K. (1970). Nature227, 680–685
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951). J. Biol. Chem.193, 265–275
Lu, R.C., Elzinga, M. (1977). Anal. Biochem.77, 243–250
Mans, R.J., Novelli, G.P. (1961). Arch. Biochem. Biophys.94, 48–53
Margulis, L., To, L., Chase, D. (1978). Science200, 1118–1124
Pierce, T., Hanson, R.K., Deanin, G.G., Gordon, M.W., Levi, A. (1978). Developmental and Biochemical Studies on Tubulin:Tyrosine Ligase. In: Maturation of Neurotransmission, A. Vernadakis, E. Giacobini, G. Filogamo eds. Basel: Karger
Raybin, D., Flavin, M. (1975). Biochem. Biophys. Res. Commun.65, 1088–1095
Raybin, D., Flavin, M. (1977). J. Cell Biol.73, 492–504
Rodriguez, J.A., Barra, H.S., Arce, C.A., Hallak, M.E., Caputto, R. (1975). Biochem. J.149, 115–121
Rodriguez, J.A., Borisy, G.G. (1978). Biochem. Biophys. Res. Commun.83, 579–586
Shelanski, M.L., Gaskin, F., Cantor, C.R. (1973). Proc. Natl. Acad. Sci. USA70, 765–768
Sloboda, R.D., Dentler, W.L., Rosenbaum, J.L. (1976). Biochem.15, 4497–4505
Snyder, J.A., McIntosh, J.R. (1976). Annu. Rev. Biochem.45, 699–720
Stephens, R.E. (1975). Structural Chemistry of the Axoneme: Evidence for Chemically and Functionally Unique Tubulin Dimers in Outer Fibers. In: Molecules and Cell Movement, S. Inoue, R.E. Stephens eds. New York: Raven Press
Stephens, R.E. (1977). Biochem.16, 2047–2058
Waterman, A.J. (1971). Chordate Structure and Function, New York: The Macmillan Co.
Wigglesworth, V.B. (1970). Insect Hormones, San Francisco: W.H. Freeman and Co.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Preston, S.F., Deanin, G.G., Hanson, R.K. et al. The phylogenetic distribution of tubulin:Tyrosine ligase. J Mol Evol 13, 233–244 (1979). https://doi.org/10.1007/BF01739482
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF01739482