A microtubule-associated protein in maize is expressed during phytochrome-induced cell elongation

被引:36
作者
Nick, P [1 ]
Lambert, AM [1 ]
Vantard, M [1 ]
机构
[1] CNRS, INST BIOL MOLEC PLANTES, F-67084 STRASBOURG, FRANCE
关键词
D O I
10.1046/j.1365-313X.1995.8060835.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Plants can adapt their shape to environmental stimuli. This response is mediated by the reorganization of cortical microtubules, a unique element of the cytoskeleton. However, the molecular base of this response has remained obscure so far. In an attempt to solve this problem, signal-dependent changes in the pattern of microtubule-binding proteins were analysed during coleoptile elongation in maize, that is, under the control of the plant photoreceptor phytochrome. Two putative MAPs of 100 kDa (P-100) and 50 kDa apparent molecular weights were identified in cytosolic extracts from non-elongating and elongating cells. Both proteins co-assembled with endogenous tubulin, bound to neurotubules and were immunologically related to the neural MAP tau: the P-100 protein, depending on the physiological situation, was manifest as a double band and was always found to be heat-stable. In contrast, the 50 kDa MAP was heat-stable only for particular tissues and physiological treatments. The P-100 protein was present in all tissues, however in a reduced amount in elongating coleoptiles. The 50 kDa MAP was expressed exclusively upon induction of phytochrome-dependent cell elongation. As shown by immunofluorescence double-staining, an epitope shared by both proteins colocalized with cortical microtubules in situ, but exclusively in elongating cells. In non-elongating cells, only the nuclei were stained. Partially purified nuclei from elongating cells were enriched in P-100, whereas the 50 kDa MAP became enriched in a partially purified plasma membrane fraction.
引用
收藏
页码:835 / 844
页数:10
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