Binding of microtubule proteins to DNA: Specificity of the interaction

Tubulin is detected among the DNA-binding proteins when an extract from fibroblasts is chromatographed on DNA-cellulose. Further purification of the colchicine-binding activity shows that purified tubulin from fibroblasts does not bind to DNA. Depolymerized brain microtubule proteins show a high affinity for DNA. The fraction bound is composed of tubulin and microtubule-associated proteins. Experiments with fractionated microtubule proteins indicate that tubulin-free microtubule-associated proteins bind to DNA, while tubulin free of microtubule-associated proteins does not. Microtubule-associated proteins bind better to eukaryotic than to phage DNA suggesting a specificity of the interaction.This work was supported by grants from the Comision Asesora para el Desarrollo de la Investigacion Cientifica y Tecnica and Comision Administradora del Descuento Complementario (I.N.P.). V.G.C. was a recipient of a fellowship of Plan de Formacion del Personal Investigador del Ministerio de Educacion y Ciencia.Peer reviewe