Identification of conserved isotype-defining variable region sequences for four vertebrate beta tubulin polypeptide classes.

Abstract

We report the determination of the complete sequences for two chicken beta tubulin genes, beta 3 and beta 5. Taken with the previously published efforts, we have determined the primary structures of five of the seven beta tubulin genes in this vertebrate species. A comparison of these sequences unambiguously reveals that amino acid sequence variations among different beta tubulin gene products are distinctly clustered within an otherwise highly conserved framework of the beta tubulin molecule. To determine the extent to which this pattern of structural heterogeneity is conserved among vertebrates, we have isolated novel beta tubulin sequences from human and mouse cDNA libraries and compared these and all other known vertebrate beta tubulin sequences with the family of chicken polypeptide sequences. What emerges from such comparison is the recognition of distinct, evolutionarily conserved isotypes of beta tubulin that are distinguished primarily by their characteristic carboxyl-terminal variable region sequence and, to a lesser extent, by sequence in an amino-terminal variable domain as well. These correlations represent a convincing demonstration that multiple beta tubulin genes in vertebrates encode a family of closely related but structurally distinct beta tubulin isotypes and further serve to define the sequences of four classes of polypeptide isotypes that constitute that family.