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Abstract
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 α-tubulin cDNA clone; B1-10, was isolated. Clone B1-10 (1493 bp) encodes for an α-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 α-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 α-tubulin. Also, the GTP binding site, which is conserved in α- and β-tubulins of different organisms, is observed in H. diminuta α-tubulin at residues 142–148. In this study the theoretical secondary and tertiary structures of H. diminuta α-tubulin protein were obtained using a computer program (3D-PSSM). (Abstract shortened by UMI.)
