4E binding proteins inhibit the translation factor eIF4E without folded structure
4E binding proteins inhibit the translation factor eIF4E without folded structure
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DOI：
10.1021/bi972494r
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发表时间：
1998-01-06
期刊：
影响因子：
2.9
通讯作者：
Wagner, G
中科院分区：
文献类型：
--
作者：
Fletcher, CM;McGuire, AM;Wagner, G
4E结合蛋白(4E-BP1和4E-BP2)通过与在大肠杆菌中产生的限制性原致癌起始因子eIF4E，4E-BPS结合来抑制翻译，核磁共振和CD测量表明，4E-BPS几乎没有折叠结构。然而，这些蛋白质抑制了网织红细胞裂解物中的翻译。此外，它们与分离的小鼠eIF4E结合，显示出一些更广泛、分散的新的核磁共振信号，但没有普遍增加化学位移分散。具有4E-BP1残基49-68残基的多肽足以与eIF4E结合并抑制网织红细胞裂解产物中的翻译，这些结果表明4E-BPS的一个短中心区域负责eIF4E的结合和翻译抑制，而其余的区域是展开的和灵活的。
The 4E binding proteins (4E-BP1 and 4E-BP2) inhibit translation by binding to the limiting, proto-oncogenic initiation factor eIF4E, 4E-BPs produced in Escherichia coli had little or no folded structure, measured by NMR and CD. However, these proteins inhibited translation in reticulocyte lysate. Furthermore, they bound to isolated mouse eIF4E, showing a few broader, dispersed new NMR signals but no general increase in chemical shift dispersion. A peptide with the sequence of 4E-BP1 residues 49-68 was sufficient to bind eIF4E and to inhibit translation in reticulocyte lysate, These results suggest that a short central region of the 4E-BPs is responsible for eIF4E binding and translation inhibition while the remainder is unfolded and flexible.