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首页> 外文期刊>Molecular and Cellular Biology >SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae.
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SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae.

机译：SUI1 / p16是酿酒酵母中真核翻译起始因子3活性所必需的。

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A genetic reversion analysis at the HIS4 locus in Saccharomyces cerevisiae has identified SUI1 as a component of the translation initiation complex which plays an important role in ribosomal recognition of the initiator codon. SUI1 is an essential protein of 12.3 kDa that is required in vivo for the initiation of protein synthesis. Here we present evidence that SUI1 is identical to the smallest subunit, p16, of eukaryotic translation initiation factor 3 (eIF-3) in S. cerevisiae. SUI1 and eIF3-p16 comigrate upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis and cross-react with anti-SUI1 and anti-eIF3 antisera. Anti-SUI1 antisera immunoprecipitate all of the subunits of eIF3, whereas antisera against the eIF3 complex and the individual PRT1 and GCD10 subunits of eIF3 immunoprecipitate SUI1. Finally, the N-terminal amino acid sequence of a truncated form of eIF3-p16 matches the sequence of SUI1. eIF3 isolated from a sui1(ts) strain at 37 degrees C lacks SUI1 and fails to exhibit eIF3 activity in the in vitro assay for methionyl-puromycin synthesis. A free form of SUI1 separate from the eIF3 complex is found in S. cerevisiae but lacks activity in the in vitro assay. The results, together with prior genetic experiments, indicate that SUI1 is essential for eIF3 activity and functions as part of eIF3 and in concert with eIF2 to promote eIF2-GTP-Met-tRNAi ternary complex recognition of the initiator codon.
机译：酿酒酵母中HIS4基因座的遗传回复分析已确定SUI1是翻译起始复合物的组成部分，该复合物在核糖体识别起始密码子中起重要作用。 SUI1是体内启动蛋白质合成所需的12.3 kDa必需蛋白质。在这里，我们提供证据表明SUI1与酿酒酵母中真核翻译起始因子3（eIF-3）的最小亚基p16相同。 SUI1和eIF3-p16通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行迁移，并与抗SUI1和抗eIF3抗血清发生交叉反应。抗SUI1抗血清免疫沉淀eIF3的所有亚基，而针对eIF3复合体的抗血清和eIF3的单个PRT1和GCD10亚基免疫沉淀SUI1。最后，截短形式的eIF3-p16的N末端氨基酸序列与SUI1的序列匹配。在37摄氏度下从sui1（ts）菌株中分离出的eIF3缺乏SUI1，并且在蛋氨酸-嘌呤霉素合成的体外测定中未显示eIF3活性。在啤酒酵母中发现了与eIF3复合体分离的SUI1游离形式，但在体外测定中缺乏活性。结果与先前的遗传实验一起表明，SUI1对于eIF3活性是必不可少的，并且是eIF3的一部分，并与eIF2协同作用以促进eIF2-GTP-Met-tRNAi三元复合物识别起始密码子。

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