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A selected ribozyme catalyzing diverse dipeptide synthesis.

Lele Sun1, Zhiyong Cui, Robert L Gottlieb

  • 1Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.

Chemistry & Biology
|May 29, 2002
PubMed
Summary
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Researchers discovered a ribozyme that synthesizes dipeptides from aminoacyl-adenylates. This finding suggests that RNA-based peptide synthesis may have preceded protein synthesis in early life.

Area of Science:

  • Origin of Life Research
  • Biochemistry
  • Molecular Evolution

Background:

  • The emergence of protein, RNA, and DNA is a fundamental question in the origin of life.
  • Aminoacyl-adenylates are current intermediates in peptide synthesis, hinting at their ancient role.
  • Uncoded peptide synthesis may have been an early evolutionary step.

Purpose of the Study:

  • To investigate the potential for RNA-based uncoded peptide synthesis.
  • To isolate and characterize ribozymes capable of peptide bond formation.
  • To explore whether ribozyme-mediated synthesis could precede coded systems.

Main Methods:

  • In vitro selection was used to isolate active peptidyl transferase ribozymes.
  • The isolated ribozymes were characterized using sequence and structural analysis.

Related Experiment Videos

  • Kinetic studies were performed to determine the efficiency of dipeptide synthesis.

    • Main Results:

    • A highly active ribozyme family capable of catalyzing dipeptide synthesis was identified.
    • The ribozyme utilized aminoacyl-adenylate substrates for peptide bond formation.
    • The ribozyme synthesized 30 different dipeptides with high efficiency, comparable to selected rates.

    Conclusions:

    • Ribozyme-mediated uncoded peptide synthesis is feasible and efficient.
    • This synthetic ribozyme provides evidence that RNA could have catalyzed peptide synthesis before genetic code development.
    • The findings support the hypothesis that ribozymes played a crucial role in early peptide formation.