PURIFICATION AND CHARACTERIZATION OF PROTEIN-SYNTHESIS INITIATION-FACTOR EIF-4E FROM THE YEAST SACCHAROMYCES-CEREVISIAE
PURIFICATION AND CHARACTERIZATION OF PROTEIN-SYNTHESIS INITIATION-FACTOR EIF-4E FROM THE YEAST SACCHAROMYCES-CEREVISIAE
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DOI：
10.1021/bi00343a009
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发表时间：
1985-01-01
期刊：
影响因子：
2.9
通讯作者：
TRACHSEL, H
中科院分区：
文献类型：
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作者：
ALTMANN, M;EDERY, I;TRACHSEL, H
通过m7 GDP-琼脂糖亲和层析从酵母酿酒酵母核糖体后上清液中纯化24，000-道尔顿蛋白[酵母真核起始因子4 E（eIF-4 E）]。该蛋白质在以下方面与哺乳动物蛋白质合成起始因子eIF-4 E的行为非常相似：（i）与m7 GDP-琼脂糖柱结合并从m7 GDP-琼脂糖柱洗脱，以及（ii）与氧化的呼肠孤病毒mRNA帽结构交联。酵母eIF-4 E是翻译所必需的，如通过针对酵母eIF-4 E的单克隆抗体对酵母提取物中的无细胞翻译的强烈和特异性抑制所示。
A 24,000-dalton protein [yeast eukaryotic initiation factor 4E (eIF-4E)] was purified from yeast Saccharomyces cerevisiae postribosomal supernatant by m7GDP-agarose affinity chromatography. The protein behaves very similarly to mammalian protein synthesis initiation factor eIF-4E with respect to (i) binding to and elution from m7GDP-agarose columns and (ii) cross-linking to oxidized reovirus mRNA cap structures. Yeast eIF-4E is required for translation as shown by the strong and specific inhibition of cell-free translation in a yeast extract by a monoclonal antibody directed against yeast eIF-4E.