Origin of Life: Chiral Short RNA Chains Capable of Non‐Enzymatic Peptide Bond Formation

Abstract

A semi-symmetric vestige of an RNA apparatus with stereochemically controlled ribozyme capabilities is embedded and functions as the site of peptide bond formation within all contemporary ribosomes, a finding that is in line with Lahav and Leiserowitz earlier discoveries on stereochemically controlled chemical reactions. As the structure of this semi-symmetrical self-folded RNA entity is almost fully conserved in all known ribosomes, it seems to be resilient to evolution, thus hinting at its pre-biotic origin and hence, suggested by us, to be the protoribosome. Recent studies, described shortly below, demonstrated peptide bond formation by the laboratory-designed protoribosomes, which supports the notion that a pre-biotic bonding entity is still functioning in all contemporary ribosomes.

The Limits of Artificial General Intelligence

“…The traditional perspective on life is that "life is chemistry" leading to the continuous search for primordial organic molecules as precursors to life [66,69], although it is then difficult to find the path of how these precursors become life. A current perspective is centered in the search for a 'protoribosome' or a primitive RNA machine capable of linking two amino acids together [64,65,68,70]. This in an attempt "to recapitulate a milestone on the road from primordial organic molecules to the ribosome used by the last common ancestor of all living things" [67] (p. 23).…”

“…They cannot explain nor create life. Therefore, all attempts to use chemistry to attempt to reproduce life are doomed to failure [64][65][66][67][68][69][70]. To quote Pattee as to what might be defined as syntactic elements in nature, "For my argument here, I will mean by matter and energy those aspects of our experience that are normally associated with physical laws" [71] (p. 213).…”

How did life begin? One key ingredient is coming into view

“…Rather than separating the reaction products by size, Bose turned to mass spectrometry, which had advanced to become the most sensitive method by this time. It still wasn't easy -she performed many reactions and control experiments, and tried two forms of mass spectrometry -but at last, she saw a peak representing the expected dipeptide 1,2 .…”

“…It's a project that other scientists have watched with interest. And the lab's achievements in the past two years -creating a primitive RNA machine that can link two amino acids together 1,2 -have created a ripple of excitement. A group in Japan, working separately and led by molecular biologist Koji Tamura at the Tokyo University of Science, has succeeded in creating a similar, functional protoribosome 3 .…”

The interplay between peptides and RNA is critical for protoribosome compartmentalization and stability

“…Based on these, several groups have proposed regions of the 23S rRNA in the large subunit, ranging approximately 100-600 nucleotides (nt) in length, as the ancestral PTC (3) (6) (7) (8) (9). Most importantly, two independent groups have recently demonstrated the peptidyl-transferase activity of their ∼70-140 nt rRNA constructs, mimicking the semi-symmetrical PTC pocket (10) (11) (12). Unlike some of the larger PTC constructs, these minimal protoribosome models were devoid of peptides, proving the rRNA sovereignty in the catalysis of amino acid polymerization.…”