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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Nonribosomal peptides are natural products with diverse bioactivities.
  • Nonribosomal peptide synthetases (NRPSs) are large enzyme complexes responsible for their biosynthesis.
  • Engineering NRPS modules offers a route to novel peptide variants.

Purpose of the Study:

  • To explore yeast display as a high-throughput screening platform for NRPS modules.
  • To assay adenylation domain activity and alter substrate specificity.
  • To demonstrate the utility of this approach for engineering NRPS specificity.

Main Methods:

  • Yeast display of NRPS elongation and termination modules (A-T and C-A-T bidomains/tridomains).
  • Assaying adenylation domain activity.
  • Reprogramming a tyrocidine synthetase module to accept a noncanonical amino acid.

Main Results:

  • Yeast display of A-T or C-A-T domains proved effective for screening.
  • Demonstrated successful alteration of substrate specificity by engineering an NRPS module.
  • Showcased the ability to incorporate noncanonical amino acids into peptides.

Conclusions:

  • Yeast display is a powerful tool for high-throughput screening and engineering of NRPSs.
  • This approach facilitates the modification of NRPS substrate specificity.
  • Enables the production of customized peptides with potentially improved properties.