血红素控制的翻译抑制剂作用模式的进一步研究：刺激蛋白在二元复合物形成水平起作用。
Further studies on the mode of action of the heme-controlled translational inhibitor: stimulating protein acts at level of binary complex formation.
作者信息
de Haro C, Ochoa S
出版信息
Proc Natl Acad Sci U S A. 1979 May;76(5):2163-4. doi: 10.1073/pnas.76.5.2163.
Abstract
Previous work has shown that (i) at physiological concentrations of eukaryotic initiation factor 2 (eIF-2), formation of the ternary complex eIF-2-GTP-Met-tRNAi, which precedes the assembly of a 40S initiation complex, requires the presence of eIF-2 stimulating protein (ESP) and (ii) the interaction of eIF-2 with ESP is blocked by the translational inhibitor which, in reticulocyte lysates, is activated in the absence of hemin. Present evidence indicates that formation of the ternary complex is preceded by formation of the binary complex eIF-2-GTP and that ESP acts at the level of binary complex formation.
摘要
先前的研究表明
（i）在真核起始因子2（eIF-2）的生理浓度下，先于40S起始复合物组装的三元复合物eIF-2-GTP-甲硫氨酰-tRNAi的形成需要eIF-2刺激蛋白（ESP）的存在；（ii）eIF-2与ESP的相互作用被翻译抑制剂阻断，在网织红细胞裂解物中，该抑制剂在无血红素的情况下被激活。目前的证据表明，三元复合物的形成之前先有二元复合物eIF-2-GTP的形成，并且ESP在二元复合物形成水平起作用。
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Binding of MET-TRNAf and GTP to homogeneous initiation factor MP.甲硫氨酰 - 转运核糖核酸f（MET-TRNAf）与鸟苷三磷酸（GTP）与均一化起始因子MP的结合。
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Additional evidence that the hemin-controlled translational repressor from rabbit reticulocytes is a protein kinase.来自兔网织红细胞的血红素控制的翻译阻遏物是一种蛋白激酶的更多证据。
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