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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G.
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The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G.

机译：真核起始因子（eIF）5 HEAT域介导多因子组装和扫描，并具有与eIF1，eIF2，eIF3和eIF4G截然不同的接口。

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摘要

Eukaryotic translation initiation factor (eIF) 5 is crucial for the assembly of the eukaryotic preinitiation complex. This activity is mediated by the ability of its C-terminal HEAT domain to interact with eIF1, eIF2, and eIF3 in the multifactor complex and with eIF4G in the 48S complex. However, the binding sites for these factors on eIF5-C-terminal domain (CTD) have not been known. Here we present a homology model for eIF5-CTD based on the HEAT domain of eIF2Bepsilon. We show that the binding site for eIF2beta is located in a surface area containing aromatic and acidic residues (aromatic/acidic boxes), that the binding sites for eIF1 and eIF3c are located in a conserved surface region of basic residues, and that eIF4G binds eIF5-CTD at an interface overlapping with the acidic area. Mutations in these distinct eIF5 surface areas impair GCN4 translational control by disrupting preinitiation complex interactions. These results indicate that the eIF5 HEAT domain is a critical nucleation core for preinitiation complex assembly and function.
机译：真核翻译起始因子（eIF）5对于真核预起始复合物的组装至关重要。此活性由其C末端HEAT域与多因子复合物中的eIF1，eIF2和eIF3以及与48S复合物中的eIF4G相互作用的能力介导。但是，这些因子在eIF5-C末端域（CTD）上的结合位点尚不清楚。在这里，我们提出了一个基于eIF2Bepsilon的HEAT域的eIF5-CTD同源模型。我们显示eIF2beta的结合位点位于包含芳香和酸性残基的表面区域（芳香/酸性盒），eIF1和eIF3c的结合位点位于碱性残基的保守表面区域，并且eIF4G与eIF5结合-CTD与酸性区域重叠的界面。这些不同的eIF5表面积突变会破坏预启动复杂的相互作用，从而损害GCN4的翻译控制。这些结果表明，eIF5 HEAT域是用于预启动复杂装配和功能的关键成核核心。

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