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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Experimental support for the evolution of symmetric protein architecture from a simple peptide motif
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Experimental support for the evolution of symmetric protein architecture from a simple peptide motif

机译：从简单的肽基序进化对称蛋白质结构的实验支持

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摘要

The majority of protein architectures exhibit elements of structural symmetry, and "gene duplication and fusion" is the evolutionary mechanism generally hypothesized to be responsible for their emergence from simple peptide motifs. Despite the central importance of the gene duplication and fusion hypothesis, experimental support for a plausible evolutionary pathway for a specific protein architecture has yet to be effectively demonstrated. To address this question, a unique "top-down symmetric deconstruction" strategy was utilized to successfully identify a simple peptide motif capable of recapitulating, via gene duplication and fusion processes, a symmetric protein architecture (the threefold symmetric β-trefoil fold). The folding properties of intermediary forms in this deconstruction agree precisely with a previously proposed "conserved architecture" model for symmetric protein evolution. Furthermore, a route through foldable sequence-space between the simple peptide motif and extant protein fold is demonstrated. These results provide compelling experimental support for a plausible evolutionary pathway of symmetric protein architecture via gene duplication and fusion processes.
机译：大多数蛋白质结构表现出结构对称性，“基因复制和融合”是通常被认为是其从简单肽基序中出现的进化机制。尽管基因复制和融合假说至关重要，但是对于特定蛋白质结构的合理进化途径的实验支持尚未得到有效证明。为了解决这个问题，采用了独特的“自上而下的对称解构”策略来成功鉴定出能够通过基因复制和融合过程概括对称蛋白质结构（三倍对称β-三叶折叠）的简单肽基序。这种解构中的中间形式的折叠特性与先前提出的对称蛋白质进化的“保守结构”模型完全一致。此外，通过简单的肽基序和现存的蛋白质折叠之间的可折叠序列空间的途径得到了证明。这些结果为通过基因复制和融合过程的对称蛋白质结构合理的进化途径提供了令人信服的实验支持。

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