M. Perez et al., A PUTATIVE BETA-TUBULIN PHOSPHATE-BINDING MOTIF IS INVOLVED IN LATERAL MICROTUBULE PROTOFILAMENT INTERACTIONS, European journal of biochemistry, 248(3), 1997, pp. 840-847
We have investigated the role of a putative GTP-binding beta-tubulin m
otif in microtubule polymerization. A peptide containing residues 126-
142 of the beta-tubulin subunit (peptide G) was synthesised and an ant
ibody against it raised. Peptide G prevents the binding of GTP to tubu
lin and also microtubule polymerization but not the formation of vinbl
astine-induced tubulin spirals, suggesting that it may prevent lateral
but not longitudinal tubulin-tubulin interactions. The antibody to pe
ptide G shows little reaction with the interphase microtubule network,
mitotic spindles or midbody of cultured cells, whereas it clearly rea
cts 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 microtu
bule structure.