Kapralou Stavroula, Fabbretti Attilio, Garulli Chiara, Spurio Roberto, Gualerzi Claudio O, Dahlberg Albert E, Pon Cynthia L
Laboratory of Genetics, Department of Biology MCA, University of Camerino, 62032 Camerino (MC), Italy.
Mol Microbiol. 2008 Dec;70(6):1368-77. doi: 10.1111/j.1365-2958.2008.06466.x. Epub 2008 Oct 2.
Bacterial translation initiation factor IF1 is homologous to archaeal aIF1A and eukaryal eIF1A, which form a complex with their homologous IF2-like factors (aIF5B and eIF5B respectively) during initiation of protein synthesis. A similar IF1-IF2 interaction is assumed to occur in all bacteria and supported by cross-linking data and stabilization of the 30S-IF2 interaction by IF1. Here we compare Escherichia coli IF1 with thermophilic factors from Bacillus stearothermophilus and Thermus thermophilus. All three IF1s are structurally similar and functionally interchangeable in vivo and in vitro. However, the thermophilic factors do not stimulate ribosomal binding of IF2DeltaN, regardless of 30S subunits and IF2 origin. We conclude that an IF1-IF2 interaction is not universally conserved and is not essential for cell survival.
细菌翻译起始因子IF1与古菌aIF1A和真核生物eIF1A同源,它们在蛋白质合成起始过程中与其同源的类IF2因子(分别为aIF5B和eIF5B)形成复合物。类似的IF1-IF2相互作用被认为在所有细菌中都会发生,并且交联数据以及IF1对30S-IF2相互作用的稳定作用也支持了这一点。在这里,我们将大肠杆菌IF1与嗜热脂肪芽孢杆菌和嗜热栖热菌的嗜热因子进行了比较。所有这三种IF1在结构上相似,并且在体内和体外功能上可互换。然而,无论30S亚基和IF2的来源如何,嗜热因子都不会刺激IF2DeltaN与核糖体的结合。我们得出结论,IF1-IF2相互作用并非普遍保守,对细胞存活也不是必需的。