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Daniel Lundin1, Gustav Berggren2, Derek T Logan3

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This study proposes a model for the origin of ribonucleotide reductase (RNR), the enzyme essential for DNA synthesis. It suggests an early RNA-protein world pathway for deoxyribonucleotide production.

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Area of Science:

  • Biochemistry
  • Molecular Evolution
  • Origin of Life

Background:

  • Deoxyribonucleotides, essential DNA building blocks, are synthesized via ribonucleotide reduction catalyzed by ribonucleotide reductase (RNR).
  • The radical-based mechanism of RNR is considered challenging for ribozyme catalysis, posing questions about early DNA precursor synthesis during the RNA-to-DNA genome transition.

Purpose of the Study:

  • To explore the evolutionary and biochemical feasibility of a ribonucleotide reductase (RNR) mechanism originating in an RNA + protein world.
  • To propose a model for a prototypical ribonucleotide reductase (protoRNR) and its evolutionary trajectory to modern RNR classes.

Main Methods:

  • Investigated the evolutionary and biochemical constraints for an early RNR mechanism.
  • Proposed a model for a prototypical RNR (protoRNR) as an ancestor to modern RNRs (urRNR).
  • Suggested a radical generation mechanism for urRNR, drawing parallels to modern class II RNRs.

Main Results:

  • A model for a prototypical ribonucleotide reductase (protoRNR) operating in an RNA + protein world is presented.
  • This protoRNR is proposed to have evolved into the urRNR, the ancestor of modern RNR classes.
  • A B12-dependent mechanism, similar to class II RNRs, is suggested for radical generation in urRNR.

Conclusions:

  • The study provides a plausible evolutionary pathway for the origin of the essential DNA synthesis enzyme, RNR.
  • The proposed model bridges the gap between early RNA-based life and the emergence of DNA genomes.
  • Understanding the evolution of RNR offers insights into the transition from RNA to DNA-based genetic systems.