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Submitted on April 20, 2004
Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4
Corresponding Author: dmuench{at}ucalgary.ca
Microtubules play an essential role in the growth and development of plants and are known to be involved in regulating many cellular processes ranging from translation to signaling. In this paper, we describe the proteomic characterization of Arabidopsis tubulin binding proteins that were purified using tubulin affinity chromatography. Microtubule co-sedimentation assays indicated that most, if not all, of the proteins in the tubulin binding protein fraction possessed microtubule-binding activity. Two-dimensional gel electrophoresis of the tubulin binding protein fraction was performed, and eighty-six protein spots were excised and analyzed for protein identification. A total of 122 proteins were identified with high confidence using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). These proteins were grouped into six categories based on their predicted functions: microtubule-associated proteins, translation factors, RNA binding proteins, signaling proteins, metabolic enzymes, and proteins with other functions. Almost one-half of the proteins identified in this fraction were related to proteins that have previously been reported to interact with microtubules. This study represents the first large-scale identification of cytoskeleton-associated proteins from a eukaryotic cell, and provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells.
Revised on July 12, 2004
Accepted on July 12, 2004
Large-scale identification of tubulin binding proteins provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells
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