Seven amino acid types suffice to reconstruct the core fold of RNA polymerase

Seven amino acid types suffice to reconstruct the core fold of RNA polymerase
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七种氨基酸类型足以重建RNA聚合酶的核心折叠

DOI:
10.1101/2021.02.22.432383
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发表时间:
2021
期刊:
Biorxiv
影响因子:
--
通讯作者:
Tagami Shunsuke
Tagami Shunsuke
中科院分区:
--
文献类型:
--
作者:
Yagi Sota;Padhi Aditya K.;Vucinic Jelena;Barbe Sophie;Schiex Thomas;Nakagawa Reiko;Simoncini David;Zhang Kam Y. J.;Tagami Shunsuke

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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.
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