Identification of a phragmoplast-associated kinesin-related protein in higher plants
Identification of a phragmoplast-associated kinesin-related protein in higher plants
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DOI：
10.1016/s0960-9822(00)00564-9
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发表时间：
2000-06-29
期刊：
影响因子：
9.2
通讯作者：
Liu, B
中科院分区：
文献类型：
--
作者：
Lee, YRJ;Liu, B
在高等植物中，膜质体执行胞质分裂。膜质的主要成分是微管，微管排列在垂直于分割平面的两个镜像阵列中[1]。这些微管的加端位于未来细胞板的位置附近。高尔基体衍生的囊泡沿着微管向正端输送，从而将材料输送到细胞板[2，3]。在细胞分裂过程中，成纤维细胞中微管的快速重组需要微管运动蛋白等微管马达蛋白的协调活动。我们克隆了拟南芥编码氨基末端运动蛋白基因AtPAKRP1的cDNA克隆，并测定了其水稻同源基因的部分序列。两组特异性抗体的免疫荧光实验表明，AtPAKRP1及其同系物在拟南芥和水稻细胞中的定位一致，在后期、末期和胞质分裂过程中，AtPAKRP1开始沿微管向纺锤体中段积累。一旦膜质微管阵列建立，AtPAKRP1就明显地定位于未来细胞板附近的微管。我们的结果为AtPAKRP1是一种迄今未知的运动提供了证据，它可能参与了膜质微管阵列的建立和/或维持。(C)2000爱思唯尔科学有限公司。保留所有权利。
The phragmoplast executes cytokinesis in higher plants. The major components of the phragmoplast are microtubules, which are arranged in two mirror-image arrays perpendicular to the division plane [1]. The plus ends of these microtubules are located near the site of the future cell plate. Golgi derived vesicles are transported along microtubules towards the plus ends to deliver materials bound for the cell plate [2,3]. During cell division, rapid microtubule reorganization in the phragmoplast requires the orchestrated activities of microtubule motor proteins such as kinesins. We isolated an Arabidopsis cDNA clone of a gene encoding an amino-terminal motor kinesin, AtPAKRP1, and have determined the partial sequence of its rice homolog. Immunofluorescence experiments with two sets of specific antibodies revealed consistent localization of AtPAKRP1 and its homolog in Arabidopsis and rice cells undergoing anaphase, telophase and cytokinesis, AtPAKRP1 started to accumulate along microtubules towards the spindle midzone during late anaphase. Once the phragmoplast microtubule array was established, AtPAKRP1 conspicuously localized to microtubules near the future cell plate. Our results provide evidence that AtPAKRP1 is a hitherto unknown motor that may take part in the establishment and/or maintenance of the phragmoplast microtubule array. (C) 2000 Elsevier Science Ltd. All rights reserved.