Characterization of a 100-kDa heat-stable microtubule-associated protein from higher plants

• Published in: European journal of biochemistry Vol. 220; no. 3; pp. 847 - 853
• Main Authors: Vantard, M, Peter, C, Fellous, A, Schellenbaum, P, Lambert, A.M
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 15-03-1994; Blackwell
• Subjects: Analytical, structural and metabolic biochemistry; Binding and carrier proteins; Biological and medical sciences; Blotting, Western; Cells, Cultured; characterization; Epitopes; Fundamental and applied biological sciences. Psychology; heat stability; Hot Temperature; Microtubule-Associated Proteins - chemistry; Microtubule-Associated Proteins - immunology; Microtubule-Associated Proteins - metabolism; microtubules; Phosphoproteins - metabolism; Phosphorylation; physicochemical properties; plant proteins; Plant Proteins - chemistry; Proteins; Tubulin - metabolism; Zea mays; Characterization; Monocotyledones; Zea mays; Antigenic determinant; Gramineae; Angiospermae; Cytoskeleton; Spermatophyta; Microtubule associated protein; Physicochemical properties
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1994.tb18687.x

In higher-plant cells, the different cell-cycle-dependent microtubule arrays are involved in a wide range of activities including chromosome segregation, cell-plate formation and cellulose microfibril distribution and orientation. A wealth of data, obtained using animal cells, has indicated that the differential stability and function of microtubules during cell-cycle and/or differentiation could be primarily regulated by selective microtubule-associated proteins (MAP). Compared to animal MAP, our knowledge of plant MAP is so far very limited. In this study, we have identified a maize heat-stable protein with apparent molecular mass 100 kDa (P-100) which binds to taxol-stabilized neurotubules and copolymerizes in vitro with purified neural tubulin. Moreover, P-100 cross-reacts with affinity-purified tau antibodies like a maize 83-kDa putative MAP described previously [Vantard, M., Schellenbaum, P., Fellous, A. & Lambert, A. M. (1991) Biochemistry 30, 9334-9340]. Polyclonal antibodies directed against P-100 were obtained and indicated that this protein is found in diverse higher-plant cultured cells suggesting the ubiquitous nature of this protein. P-100 can be phosphorylated in vitro by protein kinases present in a maize cytosol extract. Together, our data suggest that P-100 could be a higher plant MAP.