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.
D000818:Animals; D001921:Brain; D003078:Colchicine / Q000378:metabolism; D003090:Coliphages; D006224:Cricetinae; D004247:DNA / Q000378:metabolism*; D004265:DNA Helicases / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D005347:Fibroblasts; D006023:Glycoproteins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D011485:Protein Binding; D013552:Swine; D014404:Tubulin / Q000276:immunology / Q000378:metabolism*
D004279:DNA, Viral; D006023:Glycoproteins; D014404:Tubulin; D004247:DNA; D004265:DNA Helicases; D003078:Colchicine