Comparative analysis of tubulin sequences.
1. Information on the structure and evolution of tubulin has been obtained by comparing the available sequence data on 31 alpha-tubulins and 31 beta-tubulins. 2. Similar numbers of conserved amino acids are found amongst both alpha- and beta-tubulins (alpha: 48%, plus conservative substitutions: 72%; beta: 48%, plus conservative substitutions: 70%). About half of them are common to both subunits (23%, plus conservative substitutions: 45%). Four cysteines in the alpha-tubulins and 2 cysteines in the beta-tubulins are conserved. Only one cysteine (position 129) is conserved in all alpha- and beta-tubulins. 3. The longest unbroken stretch of identical amino acids between all the alpha- and beta-tubulins is found in positions 180-186 (Val-Val-Glu-Pro-Tyr-Asn), a region that appears to be important for binding the ribose moiety of GTP. Two other groups of amino acids implicated in GTP binding, one near position 70 and a glycine cluster at position 144 are also quite conserved. 4. Extra length differences between tubulin subunits, presumably present as extensions on the dimer surface, have been observed at position 50 and near position 360 in alpha-tubulins and in one case at position 57 in a beta-tubulin. 5. The introns of tubulin genes, many of them clustered in the first quarter of the tubulin coding region, do not appear to correspond to any particular structural or functional regions. 6. Mutation rates of tubulins vary considerably. The lowest alpha-tubulin homology (62.3%) is between a very divergent Drosophila alpha-tubulin and an alpha-tubulin from the yeast S. cerevisiae. The lowest beta-tubulin homology (63.3%) is between a yeast (S. cerevisiae) beta-tubulin and a mouse beta-tubulin expressed in hematopoietic tissue. In contrast, some mammalian and bird tubulins are almost identical. 7. Tubulin's heterogeneous C-termini are useful for identifying corresponding tubulins of different vertebrate species, many of which are remarkably conserved. Exceptions are the divergent beta-tubulins of erythrocyte and thrombocyte marginal bands. 8. We have proposed a model for tubulin evolution in metazoan organisms in which the release of structural constraints after gene duplication is a major cause of relatively rapid change.
Little
M
M
Institute of Cell and Tumor Biology, German Cancer Research Center, FRG.
Seehaus
T
T
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002454:Cell Differentiation; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013045:Species Specificity; D014404:Tubulin / Q000235:genetics* / Q000502:physiology
D014404:Tubulin