A Glycolytic Enzyme Binding Domain on Tubulin

Abstract

Cleavage of tubulin at tryptophan residues yielded several peptides, one of which strongly interacted with aldolase as determined by inhibition of aldolase activity. This peptide was identified as the C-terminal, residues 408–451, of the α-subunit of tubulin. Peptides with identical sequences to the C-terminal regions of the α- and β-subunits of tubulin were synthesized to further characterize interactions with glycolytic enzymes. A 43-amino-acid C-terminal peptide from α-tubulin (residues 409–451) was found to have binding properties similar to those of native tubulin and was designated the tubulin glycolytic enzyme binding domain (T-GEBD-43mer).