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Seven Amino Acid Types Suffice to Create the Core Fold of RNA Polymerase
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2021-09-24 , DOI: 10.1021/jacs.1c05367
Sota Yagi 1 , Aditya K Padhi 1 , Jelena Vucinic 2, 3, 4 , Sophie Barbe 3 , Thomas Schiex 2 , Reiko Nakagawa 5 , David Simoncini 4 , Kam Y J Zhang 1 , Shunsuke Tagami 1
Affiliation  

The extant complex proteins must have evolved from ancient short and simple ancestors. The double-ψ β-barrel (DPBB) is one of the oldest protein folds and conserved in various fundamental enzymes, such as the core domain of RNA polymerase. Here, by reverse engineering a modern DPBB domain, we reconstructed its plausible evolutionary pathway started by “interlacing homodimerization” of a half-size peptide, followed by gene duplication and fusion. Furthermore, by simplifying the amino acid repertoire of the peptide, we successfully created the DPBB fold with only seven amino acid types (Ala, Asp, Glu, Gly, Lys, Arg, and Val), which can be coded by only GNN and ARR (R = A or G) codons in the modern translation system. Thus, the DPBB fold could have been materialized by the early translation system and genetic code.

中文翻译:

七种氨基酸类型足以创建 RNA 聚合酶的核心折叠

现存的复杂蛋白质一定是从古代短而简单的祖先进化而来的。双ψ β-桶 (DPBB) 是最古老的蛋白质折叠之一,并且在各种基本酶中保守,例如 RNA 聚合酶的核心结构域。在这里,通过对现代 DPBB 结构域进行逆向工程,我们重建了其合理的进化途径,该途径从半大小肽的“交错同源二聚化”开始,然后是基因复制和融合。此外,通过简化肽的氨基酸库,我们成功地创建了只有七种氨基酸类型(Ala、Asp、Glu、Gly、Lys、Arg 和 Val)的 DPBB 折叠,它们只能由 GNN 和 ARR 编码现代翻译系统中的(R = A 或 G)密码子。因此,早期的翻译系统和遗传密码可能已经实现了 DPBB 折叠。
更新日期:2021-10-06
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