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Journal Article

One-step purification of assembly-competent tubulin from diverse eukaryotic sources.

MPS-Authors
/persons/resource/persons219787

Widlund,  Per
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Podolski,  Marija
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219566

Reber,  Simone
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons218965

Alper,  Joshua
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219702

Storch,  Marko
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219253

Hyman,  Anthony
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219249

Howard,  Jonathon
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219118

Drechsel,  David N.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Widlund, P., Podolski, M., Reber, S., Alper, J., Storch, M., Hyman, A., et al. (2012). One-step purification of assembly-competent tubulin from diverse eukaryotic sources. Molecular Biology of the Cell, 23(22), 4393-4401.


Cite as: https://hdl.handle.net/21.11116/0000-0001-087C-C
Abstract
We have developed a protocol that allows rapid and efficient purification of native, active tubulin from a variety of species and tissue sources by affinity chromatography. The affinity matrix comprises a bacterially expressed, recombinant protein, the TOG1/2 domains from Saccharomyces cerevisiae Stu2, covalently coupled to a Sepharose support. The resin has a high capacity to specifically bind tubulin from clarified crude cell extracts, and, after washing, highly purified tubulin can be eluted under mild conditions. The eluted tubulin is fully functional and can be efficiently assembled into microtubules. The method eliminates the need to use heterologous systems for the study of microtubule-associated proteins and motor proteins, which has been a major issue in microtubule-related research.