Identification and partial purification of calmodulin-binding microtuble-associated proteins from Neurospora crassa
1994
Ortega Perez, R. | Irminger-Finger, I. | Arrighi, J.F. | Capelli, N. | Tuinen, D. van | Turian, G.
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.
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