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Thioesters Support Efficient Protein Biosynthesis by the Ribosome.

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This study shows that thioesters can replace oxo-esters in transfer RNAs (tRNAs) for protein synthesis. This discovery broadens the possibilities for creating novel polymers using the cell

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Area of Science:

  • Biochemistry
  • Astrobiology
  • Synthetic Biology

Background:

  • Thioesters are vital intermediates in biological reactions and proposed for early Earth peptide synthesis.
  • The ribosome utilizes oxo-ester acyl-tRNA substrates for protein biosynthesis.
  • Investigating thioester compatibility with the ribosome is key to understanding early life and synthetic biology.

Purpose of the Study:

  • To determine if thioesters can substitute for oxo-esters in acyl-tRNA substrates during ribosomal protein synthesis.
  • To explore the potential of thioester-modified tRNAs for incorporating diverse amino acids.

Main Methods:

  • Synthesis of 3'-thio-3'-deoxyadenosine triphosphate from xylose.
  • Enzymatic modification of truncated tRNAs using the *Escherichia coli* CCA-adding enzyme.
  • Preparation of various 3'-thio-tRNAs acylated with natural and non-natural amino acids.
  • In vitro translation assays using wild-type *E. coli* ribosomes.

Main Results:

  • 3'-thio-3'-deoxyadenosine triphosphate is a substrate for the *E. coli* CCA-adding enzyme.
  • A range of 3'-thio-tRNAs were successfully synthesized and acylated.
  • *E. coli* ribosomes efficiently utilized these thio-tRNAs to produce oligopeptides.
  • Oligopeptide yields were comparable to those obtained with native oxo-ester tRNAs.

Conclusions:

  • Thioester-containing tRNAs are compatible with the extant ribosomal machinery for protein synthesis.
  • This finding supports the role of thioesters in prebiotic chemistry and expands possibilities for synthetic polymer generation.
  • The translational machinery can be leveraged to incorporate both natural and noncanonical amino acids via thioester linkages.