Szponarski W, Peltier J B, Tena G, Rossignol M
Biochimie et Physiologie Moléculaire des Plantes, INRA/ENSA-M/CNRS URA 2133, Montpellier, France.
Biochem Mol Biol Int. 1997 Nov;43(4):813-21. doi: 10.1080/15216549700204631.
Auxin binding by tobacco plasma membrane proteins was investigated. After photolabeling with [3H]IAA, 350 polypeptides were resolved on 2D gels and analyzed. Thirteen polypeptides were selected according to physico-chemical criteria. The labeling of three of them was further shown to increase, after treatment of cells with auxin, specifically in that plasma membrane subfraction where the sensitivity to the hormone of the H(+)-ATPase is enhanced by the treatment of cells. These polypeptides were those that exhibited the more specific labeling features according to physico-chemical criteria. They had similar apparent molecular weight (ca 14 kDa) that distinguished them from other auxin-binding proteins described up to now, and exhibited similar amino acid compositions. These 14 kDa polypeptides are proposed to constitute a group of new auxin-binding proteins, potentially involved, within specialized plasma membrane domains, in the stimulation of the proton pump by the hormone.
对烟草质膜蛋白与生长素的结合进行了研究。用[3H]吲哚乙酸进行光标记后，在二维凝胶上分离并分析了350种多肽。根据物理化学标准选择了13种多肽。其中三种多肽的标记在生长素处理细胞后进一步显示增加，特别是在质膜亚组分中，通过细胞处理，H(+) -ATP酶对激素的敏感性增强。这些多肽是根据物理化学标准表现出更特异性标记特征的那些。它们具有相似的表观分子量（约14 kDa），这使它们与迄今描述的其他生长素结合蛋白区分开来，并表现出相似的氨基酸组成。这些14 kDa多肽被认为构成了一组新的生长素结合蛋白，可能在特定的质膜区域内参与激素对质子泵的刺激作用。
