In plant cells, microtubule-based motor proteins have not been characterized to the same degree as in animal cells; therefore, it is not yet clear whether the movement of organelles and vesicles is also dependent on the microtubular cytoskeleton. In this work the kinesin-immunoreactive homologue from pollen tubes of Nicotiana tabacum L. has been purified and biochemically characterized. The protein preparation mainly contained a polypeptide with a relative molecular weight of approx. 100 kDa. This polypeptide bound to animal microtubules in an ATP-dependent manner and it further co-purified with an ATPase activity fourfold-stimulated by the presence of microtubules. In addition, the sedimentation coefficient (approx. 9S) was similar to those previously shown for other kinesins. Immunofluorescence analyses revealed a partial co-distribution of the protein with microtubules in the pollen tube. These data clearly indicate that several properties of the kinesin-immunoreactive homologue are similar to those of kinesin proteins, and suggest that molecular mechanisms analogous to those of animal cells may drive the microtubule-based motility of organelles and vesicles in plants.
|Titolo:||The kinesin-immunoreactive homologue from Nicotiana tabacum pollen tube: biochemical properties and subcellular localization|
|Citazione:||Cai, G., Bartalesi, A., DEL CASINO, C., Moscatelli, A., Tiezzi, A., & Cresti, M. (1993). The kinesin-immunoreactive homologue from Nicotiana tabacum pollen tube: biochemical properties and subcellular localization. PLANTA, 191(4), 496-506.|
|Appare nelle tipologie:||1.1 Articolo in rivista|