The phylogenetic distribution of tubulin:tyrosine ligase.
The post-translational addition of tyrosine to alpha-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 into alpha 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 post-translationally modified with phenylalanine or dihydroxyphenylalanine under conditions suitable for the incorporation of these compounds by vertebrate alpha tubulin.
D000818:Animals; D002347:Carps; D001517:Coleoptera / Q000201:enzymology; D049832:Decapodiformes; D008116:Lizards; D008121:Nephropidae; D010453:Peptide Synthases / Q000032:analysis*; D010802:Phylogeny; D012455:Salamandridae; D013045:Species Specificity; D014404:Tubulin; D014443:Tyrosine
D014404:Tubulin; D014443:Tyrosine; D010453:Peptide Synthases