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Journal of Molecular Evolution

, Volume 13, Issue 3, pp 233–244 | Cite as

The phylogenetic distribution of tubulin:Tyrosine ligase

  • S. F. Preston
  • G. G. Deanin
  • R. K. Hanson
  • M. W. Gordon
Article

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.

Key words

Tubulin:tyrosine ligase Microtubules Cytoskeleton Tubulin post-translational modification 

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Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • S. F. Preston
    • 1
    • 2
  • G. G. Deanin
    • 1
    • 2
  • R. K. Hanson
    • 1
  • M. W. Gordon
    • 1
    • 2
  1. 1.Ribicoff Research CenterNorwich HospitalNorwichUSA
  2. 2.Department of Biobehavioral SciencesUniversity of ConnecticutStorrsUSA

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