Cited by 24Origins and Evolution of LifeRNA and protein synthesis mechanismsEvolution and Genetic Dynamics

Possible Emergence of Sequence Specific RNA Aminoacylation via Peptide Intermediary to Initiate Darwinian Evolution and Code through Origin of Life

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Kunnev, Dimiter, Gospodinov, Anastas·2018·Life

Abstract

One of the most intriguing questions in biological science is how life originated on Earth. A large number of hypotheses have been proposed to explain it, each putting an emphasis on different events leading to functional translation and self-sustained system. Here, we propose a set of interactions that could have taken place in the prebiotic environment. According to our hypothesis, hybridization-induced proximity of short aminoacylated RNAs led to the synthesis of peptides of random sequence. We postulate that among these emerged a type of peptide(s) capable of stimulating the interaction between specific RNAs and specific amino acids, which we call “bridge peptide” (BP). We conclude that translation should have emerged at the same time when the standard genetic code begun to evolve due to the stabilizing effect on RNA-peptide complexes with the help of BPs. Ribosomes, ribozymes, and the enzyme-directed RNA replication could co-evolve within the same period, as logical outcome of RNA-peptide world without the need of RNA only self-sustained step.

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Crossref · 10.3390/life8040044

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108 of 108 references verified0 citation errors · 0 not checkable

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  • The ribozyme would give rise to pre-tRNA, and the bridge peptide to pre-aaRS.

    “Eventually, the ribozyme would give rise to pre-tRNA, and the bridge peptide to pre-aaRS [24].”

    From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [24]

    The Introduction proposes the bridge peptide as an early form in aaRS evolution, supporting the pre-aaRS half of the claim. Section 2.8 says aminoacylated RNAs would specialize into tRNAs, but it does not identify a ribozyme as the precursor of proto-tRNA. Section 2.3 mentions ribozymes as possible participants in RNA aminoacylation, not as tRNA ancestors; page numbers are unavailable in our copy. (LLM, conf=0.85)

    Experimental — accuracy not yet measured
  • The emergence of the bridge peptide facilitated the aminoacylation of RNA to specific amino acid.

    “One of the early manifestations of the transition from peptide to protein is the emergence of the ‘bridge peptide’ that facilitated the aminoacylation of RNA to specific amino acid.”

    From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [24]

    The Introduction and §2.5 propose that a “bridge peptide” facilitated RNA aminoacylation by attracting a particular amino acid. The paper presents this as a hypothesis with initially low specificity, whereas the citing sentence states its emergence and effect as fact. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • Hybridization-induced proximity of short aminoacylated RNAs led to the emergence of bridge peptides, which were capable of stimulating the interaction between specific RNAs and specific amino acids.

    “Hybridization-induced proximity of short aminoacylated RNAs led to the emergence of bridge peptides, which were capable of stimulating the interaction between specific RNAs and specific amino acids [24].”

    From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [24]

    The Introduction postulates that bridge peptides arose from the proximity of hybridized, short aminoacylated RNAs. Section 2.5 proposes that such peptides could bring specific amino acids near RNA and facilitate aminoacylation. The citing sentence presents this proposed origin-of-life scenario as an established event rather than a hypothesis. (LLM, conf=0.86)

    Experimental — accuracy not yet measured
  • The evolution of peptides to proteins occurred from a small motif of short peptides to longer folded peptides, and finally to proteins that form complex catalytic centers with almost unlimited possible functions.

    “The evolution of peptides to proteins occurred from a small motif of short peptides to longer folded peptides, and finally to proteins that form complex catalytic centers with almost unlimited possible functions [24].”

    From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [24]

    Section 2.8, “Step 7. the Evolution of Functions,” describes the proposed progression from small motifs to folded proteins and increasingly complex catalytic functions. It says this evolution “would occur,” however, while the citing sentence presents it as something that occurred. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • Initially, one kind of an amino acid and one kind of hairpin would be catalyzed by an activating enzyme, perhaps a precursor to the aminoacyl transfer tRNA synthetase, such as bridge peptide.

    “Initially, one kind of an amino acid and one kind of hairpin would be catalyzed by an activating enzyme, perhaps a precursor to the aminoacyl transfer tRNA synthetase, such as bridge peptide, which is a very short peptide that facilitated the emergence of self-sustained RNA-peptide complex supporting a primitive translation [24].”

    From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [24]

    The Introduction proposes a short bridge peptide as a precursor of aminoacyl-tRNA synthetases that facilitated RNA aminoacylation and primitive translation. But §2.3 describes initial aminoacylation as non-enzymatic or potentially ribozyme-assisted, involving any RNA and amino acids without the claimed one-amino-acid, one-hairpin pairing. The paper does not describe an initial activating enzyme catalyzing that specific pair. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

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Authors
Kunnev, D., & Gospodinov, A.
Affiliations
  • Roswell Park Comprehensive Cancer Center (US)
  • Bulgarian Academy of Sciences (BG)
Corresponding author
Gospodinov, Anastas
Venue
Life
Publisher
MDPI AG
Published
2018-10-02
Volume
8
Issue
4
Pages
44
ISSN
2075-1729 (ISSN-L)
OpenAlex
W2895774178
Cited by
24
References
108
Citations by year
2025: 1 · 2024: 1 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 10 · 2019: 3
FWCI
2.01
Type
journal article
Language
en
Open access
Locations
  • Life (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, other-oa)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
Keywords
origin of life, peptide intermediates, genetic code evolution, nucleic acid hybridization, prebiotic peptide synthesis, ribozymes

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