COASSEMBLY PROPERTIES OF HIGHER-PLANT MICROTUBULE-ASSOCIATED PROTEINS WITH PURIFIED BRAIN AND PLANT TUBULINS

The knowledge of higher plant microtubule-associated proteins (MAPs) remains limited to a few examples that illustrate essentially their binding properties to preformed microtubules as described in carrots. Using taxol-stabilized microtubules a putative MAP-enriched fraction has been isolated in maize cultured cell extracts, one of these polypeptides is immunologically related to neural tau. At present, these proteins are being characterized by co-assembly assays that were not possible before. Similar experiments were done also in a heterologous system using brain tubulin. Three polypeptides out of seven that constituted the MAP fraction were found to co-assemble specifically with tubulin subunits of both origins. Their apparent molecular weights are 67, 83 and 125 kDa. A two-dimensional gel immunoblot of the 83 kDa polypeptide with tau antibodies revealed one major spot. Polypeptides were quantiated by scanning the gels. These results shed light on the present debate on higher plant MAPs and their potential activity in the regulation of microtubule assembly and function in the higher plant cell.