Plant 115-kDa actin-filament bundling protein, P-115-ABP, is a homologue of plant villin and is widely distributed in cells.

Plant 115-kDa actin-filament bundling protein, P-115-ABP, is a homologue of plant villin and is widely distributed in cells.
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DOI:
10.1093/pcp/pcg132
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发表时间:
2003-10
影响因子:
4.9
通讯作者:
E. Yokota;L. Vidali;M. Tominaga;H. Tahara;H. Orii;Yosuke Morizane;P. K. Hepler;T. Shimmen
E. Yokota;L. Vidali;M. Tominaga;H. Tahara;H. Orii;Yosuke Morizane;P. K. Hepler;T. Shimmen
中科院分区:
生物学2区
文献类型:
--
作者:
E. Yokota;L. Vidali;M. Tominaga;H. Tahara;H. Orii;Yosuke Morizane;P. K. Hepler;T. Shimmen

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在许多情况下,肌动蛋白细丝排列成束,并作为植物细胞中细胞质流动的轨迹。我们从百合萌发花粉中分离到一种肌动蛋白-丝束蛋白,由115 kDa多肽(P-115-ABP)组成。(1998)生物化学:生物物理学。[中英文摘要]Re.Commun.249:61]。P-115-ABP与维林蛋白的植物同源物植物135 kDa肌动蛋白-细丝束蛋白(P-135-ABP)具有相似的抗原性。一个全长cdna克隆(ABP115;登录号:AB097407)是用P-115-ABP和P-135-ABP抗血清免疫筛选从百合花粉表达文库中分离得到的。由该克隆推导的P-115-ABP的氨基酸序列与拟南芥的P-135-ABP和4种绒毛蛋白亚型(AtVLN1、AtVLN2、AtVLN3和AtVLN4)特别是AtVLN4有很高的同源性,表明P-115-ABP也可以归类为植物绒毛蛋白。从百合萌发花粉中生化分离的P-115-ABP能够将极性均匀的F-肌动蛋白纤维排列成束状,这种排列活性可被钙-钙调蛋白(CaM)抑制,这与P-135-ABP的肌动蛋白-细丝束性质相似。P-115-ABP型植物绒毛蛋白广泛分布于植物细胞中,从藻类到陆地植物。在水葫芦的根毛细胞中,这种类型的植物绒毛蛋白与肌动蛋白-细丝束共同定位于跨液泡束和皮质下区域。将P-115-ABP抗血清微量注射到活的根毛细胞中,可引起横空链的消失和细胞质流动途径的改变。在缺乏P-135-ABP型植物绒毛蛋白的珊瑚轮节间细胞中,P-115-ABP型与锚定在叶绿体细胞内表面的肌动蛋白-细丝缆索共定位。这些结果表明,植物绒毛广泛分布于整个植物界,并参与肌动蛋白细丝成束的组织。
In many cases, actin filaments are arranged into bundles and serve as tracks for cytoplasmic streaming in plant cells. We have isolated an actin-filament bundling protein, which is composed of 115-kDa polypeptide (P-115-ABP), from the germinating pollen of lily, Lilium longiflorum [Nakayasu et al. (1998) BIOCHEM: Biophys. Res. Commun. 249: 61]. P-115-ABP shared similar antigenicity with a plant 135-kDa actin-filament bundling protein (P-135-ABP), a plant homologue of villin. A full-length cDNA clone (ABP115; accession no. AB097407) was isolated from an expression cDNA library of lily pollen by immuno-screening using antisera against P-115-ABP and P-135-ABP. The amino acid sequence of P-115-ABP deduced from this clone showed high homology with those of P-135-ABP and four villin isoforms of Arabidopsis thaliana (AtVLN1, AtVLN2, AtVLN3 and AtVLN4), especially AtVLN4, indicating that P-115-ABP can also be classified as a plant villin. The P-115-ABP isolated biochemically from the germinating lily pollen was able to arrange F-actin filaments with uniform polarity into bundles and this bundling activity was suppressed by Ca2+-calmodulin (CaM), similar to the actin-filament bundling properties of P-135-ABP. The P-115-ABP type of plant villin was widely distributed in plant cells, from algae to land plants. In root hair cells of Hydrocharis dubia, this type of plant villin was co-localized with actin-filament bundles in the transvacuolar strands and the sub-cortical regions. Microinjection of the antiserum against P-115-ABP into living root hair cells caused the disappearance of transvaculor strands and alteration of the route of cytoplasmic streaming. In internodal cells of Chara corallina in which the P-135-ABP type of plant villin is lacking, the P-115-ABP type showed co-localization with actin-filament cables anchored on the intracellular surface of chloroplasts. These results indicated that plant villins are widely distributed and involved in the organization of actin filaments into bundles throughout the plant kingdom.