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真核生物起始因子4A在帽识别过程中的作用。

Involvement of eukaryotic initiation factor 4A in the cap recognition process.

作者信息

Edery I, Hümbelin M, Darveau A, Lee K A, Milburn S, Hershey J W, Trachsel H, Sonenberg N

出版信息

J Biol Chem. 1983 Sep 25;258(18):11398-403.

PMID:6604056
Abstract

Antibodies against eukaryotic initiation factor 4A (eIF-4A) were used to study the involvement of this factor in recognizing the 5' cap structure of eukaryotic mRNA. We demonstrate that an approximately 50-kilodalton polypeptide present in rabbit reticulocyte ribosomal high salt wash which can be specifically cross-linked to the 5' oxidized cap structure of reovirus mRNA (Sonenberg, N. (1981) Nucleic Acids Res. 9, 1643) reacts with an anti-eIF-4A monoclonal antibody. We also show that antibodies against eIF-4A react with a 50-kilodalton polypeptide present in a cap-binding protein complex obtained by elution from a m7GTP-agarose affinity column. Comparative peptide analysis of eIF-4A and the 50-kilodalton component of the cap-binding protein complex indicates a very strong similarity between the two polypeptides.

摘要

针对真核起始因子4A(eIF - 4A)的抗体被用于研究该因子在识别真核mRNA 5'帽结构中的作用。我们证明,存在于兔网织红细胞核糖体高盐洗脱液中的一种约50千道尔顿的多肽,它可与呼肠孤病毒mRNA的5'氧化帽结构特异性交联(索嫩伯格,N.(1981年)《核酸研究》9,1643),能与抗eIF - 4A单克隆抗体发生反应。我们还表明,针对eIF - 4A的抗体与通过从m7GTP - 琼脂糖亲和柱洗脱获得的帽结合蛋白复合物中存在的一种50千道尔顿的多肽发生反应。对eIF - 4A和帽结合蛋白复合物的50千道尔顿组分进行的肽段比较分析表明,这两种多肽之间有非常强的相似性。

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