Identification and partial purification of calmodulin-binding microtubule-associated proteins from Neurospora crassa.
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.
Ortega Perez
R
R
Laboratory of General Microbiology, University of Geneva, Switzerland.
Irminger-Finger
I
I
Arrighi
J F
JF
Capelli
N
N
van Tuinen
D
D
Turian
G
G
D000906:Antibodies / Q000276:immunology; D000918:Antibody Specificity; D015153:Blotting, Western; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism*; D002846:Chromatography, Affinity; D004355:Drug Stability; D006358:Hot Temperature; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D009492:Neurospora crassa / Q000737:chemistry*; D013379:Substrate Specificity
D000906:Antibodies; D002147:Calmodulin; D008869:Microtubule-Associated Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases