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Putative one-pot prebiotic polypeptides with ribonucleolytic activity

机译：推定的一锅具有核糖核酸分解活性的益生元多肽

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摘要

KIA7, a peptide with a highly restricted set of amino acids (Lys, Ile, Ala, Gly and Tyr), adopts a specifically folded structure. Some amino acids, including Lys, Ile, Ala, Gly and His, form under the same putative prebiotic conditions, whereas different conditions are needed for producing Tyr, Phe and Trp. Herein, we report the 3D structure and conformational stability of the peptide KIA7H, which is composed of only Lys, Ile, Ala, Gly and His. When the imidazole group is neutral, this 20-mer peptide adopts a four-helix bundle with a specifically packed hydrophobic core. Therefore, one-pot prebiotic proteins with well-defined structures might have arisen early in chemical evolution. The Trp variant, KIA7W, was also studied. It adopts a 3D structure similar to that of KIA7H and its previously studied Tyr and Phe variants, but is remarkably more stable. When tested for ribonucleolytic activity, KIA7H, KIA7W and even short, unstructured peptides rich in His and Lys, in combination with Mg~(++), Mn ~(+ +) or Ni~(++) (but not Cu~(+ +), Zn~(++) or EDTA) specifically cleave the single-stranded region in an RNA stem-loop. This suggests that prebiotic peptide-divalent cation complexes with ribonucleolytic activity might have coinhabited the RNA world.
机译：KIA7是具有高度限制的一组氨基酸（Lys，Ile，Ala，Gly和Tyr）的肽，采用特定折叠的结构。某些氨基酸（包括Lys，Ile，Ala，Gly和His）在相同的益生元条件下形成，而产生Tyr，Phe和Trp需要不同的条件。本文中，我们报告了仅由Lys，Ile，Ala，Gly和His组成的KIA7H肽的3D结构和构象稳定性。当咪唑基为中性时，此20-mer肽采用带有特殊堆积的疏水核的四螺旋束。因此，一罐结构明确的益生元蛋白质可能在化学进化的早期就出现了。还研究了Trp变体KIA7W。它采用类似于KIA7H及其先前研究的Tyr和Phe变体的3D结构，但明显更稳定。当测试其核糖核酸水解活性时，与Mg〜（++），Mn〜（++）或Ni〜（++）结合使用时，KIA7H，KIA7W甚至富含His和Lys的短的，非结构化的短肽（但不包括Cu〜（ + +，Zn〜（++）或EDTA）特异性切割RNA茎环中的单链区域。这表明具有核糖核酸分解活性的益生元肽二价阳离子复合物可能与RNA世界并存。

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