Characterization of maize microtubule-associated proteins, one of which is immunologically related to tau

• Published in: Biochemistry (Easton) Vol. 30; no. 38; pp. 9334 - 9340
• Main Authors: Vantard, Marylin, Schellenbaum, Paul, Fellous, Arlette, Lambert, Anne Marie
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-09-1991
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Binding and carrier proteins; Biological and medical sciences; Blotting, Western; Brain - ultrastructure; Cells, Cultured; Cross Reactions; Fundamental and applied biological sciences. Psychology; In Vitro Techniques; microtubule-associated proteins; Microtubule-Associated Proteins - chemistry; Microtubule-Associated Proteins - immunology; Microtubule-Associated Proteins - isolation & purification; microtubules; Microtubules - chemistry; Microtubules - ultrastructure; Plant Proteins - immunology; Polymers; Proteins; Species Specificity; Swine; Tau protein; tau Proteins; Tubulin - metabolism; Zea mays - analysis; Corn; Identification; Electron microscopy; Pig; Vertebrata; Mammalia; Molecular assembly; Microtubule associated protein; Artiodactyla; Microtubule; Mechanism of action; Ungulata; Brain (vertebrata)
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00102a028

Microtubule-associated proteins (MAPs) are identified as proteins that copurify with tubulin, promote tubulin assembly, and bind to microtubules in vitro. Higher plant MAPs remain mostly unknown. One example of non-tubulin carrot proteins, which bind to neural microtubules and induce bundling, has been reported so far [Cyr, R. J., & Palewitz, B. A. (1989) Planta 177, 245-260]. Using taxol, we developed an assay where higher plant microtubules were induced to self-assemble in cytosolic extracts of maize cultured cells and were used as the native matrix to isolate putative plant MAPs. Several polypeptides with an apparent molecular masses between 170 and 32 kDa copolymerized with maize microtubules. These putative maize MAPs also coassembled with pig brain tubulin through two cycles of temperature-dependent assembly-disassembly. They were able to initiate and promote MAP-free tubulin assembly under conditions of nonefficient self-assembly and induced bundling of both plant and neural microtubules. One of these proteins, of about 83 kDa, cross-reacted with affinity-purified antibodies against rat brain tau proteins, suggesting the presence of common epitope(s) between neural tau and maize proteins. This homology might concern the tubulin-binding domain, as plant and neural tubulins are highly conserved and the plant polypeptides coassembled with brain tubulin.