Functional complementation by wheat elF2α in the yeast GCN2-mediated pathway
Functional complementation by wheat elF2α in the yeast GCN2-mediated pathway
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DOI：
10.1006/bbrc.2000.3964
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发表时间：
2000-12-20
影响因子：
3.1
通讯作者：
Roth, D
中科院分区：
文献类型：
--
作者：
Chang, LY;Yang, WY;Roth, D
通过丝氨酸51上的特异性eIF2 α磷酸化的翻译控制已经在所有真核生物中表征，植物是显著的例外。为了评估植物eIF2 α功能性控制翻译的能力，在酵母遗传系统中表达小麦eIF2 α的野生型（51S）和不可磷酸化的突变体（51A）。在抑制eIF2 α磷酸化途径的条件下，任一小麦蛋白的表达都不会阻碍生长。然而，在诱导特异性eIF2 α磷酸化的条件下，只有表达小麦51S的菌株能够生长2至4天。生长依赖于酵母eIF2 α激酶GCN 2的活性，并导致GCN 4的翻译增加。植物eIF2 α和酵母eIF2B之间的关联得到转基因酵母细胞特异性免疫共沉淀的支持。这些数据支持真核生物翻译起始过程之间的相似性，并加强了植物可能含有eIF2 α磷酸化途径的概念。(C)北京大学出版社.
Translational control by specific eIF2 alpha phosphorylation on serine 51 has been characterized in all eukaryotes with the significant exception of plants. In order to evaluate the capability of plant eIF2 alpha to functionally control translation, the wild type (51S) and a nonphosphorylatable mutant (51A) of wheat eIF2 alpha were expressed in a yeast genetic system. Expression of either wheat protein did not handicap growth under conditions that repress the eIF2 alpha phosphorylation pathway. However, under conditions that induce specific eIF2 alpha phosphorylation only strains expressing wheat 51S were able to grow between 2 and 4 days. Growth was dependent upon activity of yeast, eIF2 alpha kinase GCN2 and resulted in the increased translation of GCN4. The association between plant eIF2 alpha and yeast eIF2B is supported by their specific coimmunoprecipitation from transgenic yeast cells. These data support the similarity among eukaryotic translational initiation processes and strengthen the concept that plants may contain an eIF2 alpha phosphorylation pathway. (C) 2000 Academic Press.