Two novel intrinsic annexins accumulate in wheat membranes in response to low temperature
Two novel intrinsic annexins accumulate in wheat membranes in response to low temperature
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DOI：
10.1093/pcp/41.2.177
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发表时间：
2000-02-01
影响因子：
4.9
通讯作者：
Sarhan, F
中科院分区：
文献类型：
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作者：
Breton, G;Vazquez-Tello, A;Sarhan, F
在冷驯化小麦(Triticum Aestivum)中鉴定出4个属于膜联蛋白家族的免疫相关蛋白。分子质量分别为34 kDa和36 kDa的两种可溶性形式以钙依赖的方式结合磷脂膜。这两种形式与之前报道的几种植物中的二倍体相似。另外两种形式，分子质量分别为39和22.5 kDa，与微体组分有关。生化分析表明，这两种形式都是固有的膜蛋白，它们与膜的结合不依赖于钙。据我们所知，这是植物中存在这些膜联蛋白形式的第一次报告。两相膜分离纯化表明，P39形式定位于质膜。免疫印迹分析显示，P39和P22.5的蛋白水平在低温暴露一天后逐渐升高，达到最高水平。蛋白质的积累在抗寒性较强的品种和抗寒性较弱的品种中都是相似的，表明这种积累与耐寒性无关。讨论了这些新的内源性膜联结蛋白在低温信号转导途径中的可能作用。
Four immunologically related proteins that belong to the annexin family were identified in cold acclimated wheat (Triticum aestivum). Two soluble forms with molecular masses of 34 and 36 kDa were found to bind phospholipid membranes in a calcium-dependent manner. These two forms are similar to the previously reported doublet in several plant species. The other two forms, with molecular masses of 39 and 22.5 kDa, were found associated with the microsomal fraction. Biochemical analysis showed that both forms are intrinsic membrane proteins and their association with the membrane is calcium independent. This is, to our knowledge, the first report of the presence of these annexin forms in plants. Membrane purification by two phase partitioning demonstrated that the p39 form is localized to the plasma membrane. Immunoblot analysis showed that the protein level of both p39 and p22.5 increases gradually reaching a maximum level after one day of low temperature exposure. The protein accumulation was similar in both hardy and less hardy cultivars, suggesting that the accumulation is not correlated with freezing tolerance. The results are discussed with respect to the possible role of these new intrinsic membrane annexins in low temperature signal transduction pathway.