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Refinement of OnePot PURE and Crude Ribosome Production for Reproducible Cell-free Protein Synthesis

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Putative one-pot prebiotic polypeptides with ribonucleolytic activity.

Jorge P López-Alonso¹, Miguel A Pardo-Cea, Irene Gómez-Pinto

¹Instituto de Química Física Rocasolano C.S.I.C. Serrano 119, 28006, Madrid, Spain.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|March 17, 2010

Summary

Prebiotic peptides like KIA7H, composed of specific amino acids, can form complex structures and exhibit RNA-cleaving activity. This suggests early protein-metal complexes may have played a role in the RNA world.

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Area of Science:

Biochemistry
Astrobiology
Origin of Life Studies

Background:

Amino acids like Lys, Ile, Ala, Gly, and His can form under prebiotic conditions.
Peptides composed of restricted amino acid sets can adopt specific folded structures.
The early RNA world may have involved interactions with prebiotic peptides.

Purpose of the Study:

To determine the 3D structure and conformational stability of the peptide KIA7H.
To investigate the ribonucleolytic activity of KIA7H and its variants.
To explore the potential role of prebiotic peptide-divalent cation complexes in early life.

Main Methods:

X-ray crystallography or NMR spectroscopy to determine 3D structure.
Circular dichroism or thermal denaturation assays for conformational stability.
In vitro assays to test ribonucleolytic activity with various divalent cations.

Main Results:

KIA7H forms a stable four-helix bundle with a hydrophobic core when its imidazole group is neutral.
The Trp variant (KIA7W) shows similar structure but enhanced stability compared to other variants.
KIA7H, KIA7W, and short His/Lys-rich peptides exhibit specific RNA cleavage in the presence of Mg(2+), Mn(2+), or Ni(2+).

Conclusions:

Well-defined peptide structures could have emerged early in chemical evolution.
Prebiotic peptides, particularly those rich in His and Lys, can possess ribonucleolytic activity.
Peptide-divalent cation complexes may have been functional components of the RNA world.