Ortega Perez R, Irminger-Finger I, Arrighi J F, Capelli N, van Tuinen D, Turian G
Laboratory of General Microbiology, University of Geneva, Switzerland.
Eur J Biochem. 1994 Dec 1;226(2):303-10. doi: 10.1111/j.1432-1033.1994.tb20054.x.
We have purified microtubule-associated proteins from Neurospora crassa on the basis of heat stability and affinity to calmodulin. Two proteins of molecular masses 170 kDa and 190 kDa have been partially purified. A third protein of 145 kDa was purified almost to homogeneity, and we present evidence that this protein is a specific substrate for a Ca2+/calmodulin-dependent protein kinase. The purified 170-, 190-, and 145-kDa proteins induce the assembly of microtubules from purified porcine brain tubulin. We demonstrate that all three proteins are microtubule-associated proteins on the basis of an in vitro microtubule-binding assay.
