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甜菜坏死黄脉病毒的细胞间移动:I. 异源互补实验为三基因块蛋白间的特异性相互作用提供了证据。

Cell-to-cell movement of beet necrotic yellow vein virus: I. Heterologous complementation experiments provide evidence for specific interactions among the triple gene block proteins.

作者信息

Lauber E, Bleykasten-Grosshans C, Erhardt M, Bouzoubaa S, Jonard G, Richards K E, Guilley H

机构信息

Institut de Biologie Moléculaire des Plantes du CNRS et de l'Université Louis Pasteur, Strasbourg, France.

出版信息

Mol Plant Microbe Interact. 1998 Jul;11(7):618-25. doi: 10.1094/MPMI.1998.11.7.618.

DOI:10.1094/MPMI.1998.11.7.618
PMID:9650295
Abstract

Cell-to-cell movement of beet necrotic yellow vein virus (BNYVV) requires three proteins encoded by a triple gene block (TGB) on viral RNA 2. A BNYVV RNA 3-derived replicon was used to express movement proteins to functionally substitute for the BNYVV TGB proteins was tested by coinoculation of TGB-defective BNYVV with the various replicons to Chenopodium quinoa. Trans-heterocomplementation was successful with the movement protein (P30) of tobacco mosaic virus but not with the tubule-forming movement proteins of alfalfa mosaic virus and grapevine fanleaf virus. Trans-complementation of BNYVV movement was also observed when all three TGB proteins of the distantly related peanut clump virus were supplied together but not when they were substituted for their BNYVV counterparts one by one. When P30 was used to drive BNYVV movement in trans, accumulation of the first TGB protein of BNYVV was adversely affected by null mutations in the second and third TGB proteins. Taken together, these results suggest that highly specific interactions among cognate TGB proteins are important for their function and/or stability in planta.

摘要

甜菜坏死黄脉病毒(BNYVV)的细胞间移动需要病毒RNA 2上由三基因块(TGB)编码的三种蛋白质。通过将TGB缺陷型BNYVV与各种复制子共接种到藜麦上,测试了一种源自BNYVV RNA 3的复制子表达移动蛋白以功能替代BNYVV TGB蛋白的能力。烟草花叶病毒的移动蛋白(P30)成功实现了反式异源互补,但苜蓿花叶病毒和葡萄扇叶病毒的形成管状结构的移动蛋白则未成功。当一起提供远缘相关花生丛簇病毒的所有三种TGB蛋白时,也观察到了BNYVV移动的反式互补,但当它们逐个替代BNYVV对应蛋白时则未观察到。当使用P30来反式驱动BNYVV移动时,BNYVV第一个TGB蛋白的积累受到第二个和第三个TGB蛋白无效突变的不利影响。综上所述,这些结果表明同源TGB蛋白之间高度特异性的相互作用对其在植物中的功能和/或稳定性很重要。

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