In this study, a cDNA library from Hymenolepis diminuta was constructed. This is the first cDNA library made from this organism. Using cDNA library screening a full length alpha-tubulin cDNA clone; B1-10, was isolated. Clone B1-10 (1493 bp) encodes for an alpha-tubulin of 450 amino acids with a calculated molecular weight of 49.79 kDa. This is the first tubulin sequence to be reported from an eucestode. Structural analysis of the alpha-tubulin sequence showed that putative sites for all posttranslational modifications such as detyrosination/tyrosination, phosphorylation, glycylation, glutamylation and acetylation have been conserved in H. diminuta alpha-tubulin. Also, the GTP binding site, which is conserved in alpha- and beta-tubulins of different organisms, is observed in H. diminuta alpha-tubulin at residues 142--148. In this study the theoretical secondary and tertiary structures of H. diminuta alpha-tubulin protein were obtained using a computer program (3D-PSSM). (Abstract shortened by UMI.)... |