THE KINESIN-IMMUNOREACTIVE HOMOLOG FROM NICOTIANA-TABACUM POLLEN TUBES - BIOCHEMICAL-PROPERTIES AND SUBCELLULAR-LOCALIZATION
THE KINESIN-IMMUNOREACTIVE HOMOLOG FROM NICOTIANA-TABACUM POLLEN TUBES - BIOCHEMICAL-PROPERTIES AND SUBCELLULAR-LOCALIZATION
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DOI：
10.1007/bf00195751
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发表时间：
1993-09-01
期刊：
影响因子：
4.3
通讯作者：
CRESTI, M
中科院分区：
文献类型：
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作者：
CAI, G;BARTALESI, A;CRESTI, M
在植物细胞中，基于微管的运动蛋白还没有被表征到与动物细胞相同的程度；因此，目前尚不清楚细胞器和囊泡的运动是否也依赖于微管细胞骨架。本文从烟草花粉管中分离纯化了运动蛋白免疫反应同源物，并对其进行了生化表征。该蛋白制剂主要含有相对分子量约为的多肽。100 kDa。该多肽以atp依赖的方式与动物微管结合，并进一步与微管存在时四倍刺激的atp酶活性共纯化。此外，沉降系数(约为。9S)与其他驱动蛋白相似。免疫荧光分析显示该蛋白与花粉管中的微管部分共分布。这些数据清楚地表明，激酶蛋白免疫反应同源物的一些特性与激酶蛋白相似，并表明类似于动物细胞的分子机制可能驱动植物中基于微管的细胞器和囊泡的运动。
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.