Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antibodies / immunology
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Antibody Specificity
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Blotting, Western
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism
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Calmodulin / metabolism*
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Chromatography, Affinity
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Drug Stability
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Hot Temperature
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Microscopy, Electron
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Microtubule-Associated Proteins / chemistry
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Microtubule-Associated Proteins / isolation & purification*
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Microtubule-Associated Proteins / metabolism
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Microtubules / metabolism
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Microtubules / ultrastructure
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Neurospora crassa / chemistry*
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Substrate Specificity
Substances
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Antibodies
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Calmodulin
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Microtubule-Associated Proteins
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Calcium-Calmodulin-Dependent Protein Kinases