Purification of microtubule proteins from Xenopus egg extracts: identification of a 230K MAP4-like protein.
We describe the purification of microtubule proteins from Xenopus egg extracts by temperature-dependent assembly and disassembly in the presence of dimethyl sulfoxide and identify a number of presumptive microtubule-associated proteins (MAPs). One of these proteins has a molecular weight of 230 kDa and is immunologically related to HeLa MAP4. We show that this MAP is heat stable and phosphorylated, and that it promotes elongation of microtubules from axonemes.
Faruki
S
S
Cell Biology Program, European Molecular Biology Laboratory, Heidelberg, Germany.
Karsenti
E
E
D000818:Animals; D000911:Antibodies, Monoclonal; D002923:Cilia / Q000648:ultrastructure; D003429:Cross Reactions; D004527:Egg Proteins / Q000302:isolation & purification*; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006358:Hot Temperature; D006801:Humans; D008868:Microtubule Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D008869:Microtubule-Associated Proteins / Q000032:analysis* / Q000494:pharmacology; D008870:Microtubules / Q000187:drug effects; D008970:Molecular Weight; D011485:Protein Binding; D014981:Xenopus
D000911:Antibodies, Monoclonal; D004527:Egg Proteins; D008868:Microtubule Proteins; D008869:Microtubule-Associated Proteins