Abstract

We have investigated the role of a putative GTP-binding beta-tubulin motif in microtubule polymerization. A peptide containing residues 126-142 of the beta-tubulin subunit (peptide G) was synthesised and an antibody against it raised. Peptide G prevents the binding of GTP to tubulin and also microtubule polymerization but not the formation of vinblastine-induced tubulin spirals, suggesting that it may prevent lateral but not longitudinal tubulin-tubulin interactions. The antibody to peptide G shows little reaction with the interphase microtubule network, mitotic spindles or midbody of cultured cells, whereas it clearly reacts with vinblastine-induced paracrystals. These results suggest that this putative phosphate-binding site present in beta-tubulin could be involved in the lateral tubulin-tubulin interactions along the microtubule structure.

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