A GLYCOLYTIC ENZYME BINDING DOMAIN ON TUBULIN

Cleavage of tubulin at tryptophan residues yielded several peptides, o ne of which strongly interacted with aldolase as determined by inhibit ion of aldolase activity. This peptide was identified as the C-termina l, residues 408-451, of the cw-subunit of tubulin. Peptides with ident ical sequences to the C-terminal regions of the alpha- and beta-subuni ts of tubulin were synthesized to further characterize interactions wi th glycolytic enzymes. A 43-amino-acid C-terminal peptide from alpha-t ubulin (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). (C) 1997 Academic Press.