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Hijacking a bacterial ABC transporter for genetic code expansion.

Tarun Iype1, Maximilian Fottner1, Paul Böhm1

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Researchers engineered bacterial transporters to improve cellular uptake of non-canonical amino acids (ncAAs), overcoming a key bottleneck for genetic code expansion and protein functionalization.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Site-specific incorporation of non-canonical amino acids (ncAAs) expands protein functionality but is limited by low incorporation efficiencies.
  • Poor cellular uptake of ncAAs is a major obstacle hindering efficient genetic code expansion.

Purpose of the Study:

  • To overcome the bottleneck of poor cellular uptake for enhanced ncAA incorporation.
  • To develop a novel strategy for efficient and programmable import of diverse chemical building blocks into proteins.

Main Methods:

  • Hijacked bacterial ATP-binding cassette (ABC) transporters to actively import ncAAs.
  • Utilized easily synthesizable isopeptide-linked tripeptides processed into ncAAs intracellularly.
  • Developed a high-throughput directed evolution platform to engineer transporter systems for refractory ncAAs.

Main Results:

  • Achieved efficient encoding of previously inaccessible ncAAs, enabling protein decoration with bioorthogonal moieties, crosslinkers, and post-translational modifications.
  • Engineered customized Escherichia coli strains for single and multi-site ncAA incorporation at wild-type efficiencies.
  • Adapted tripeptide scaffolds for efficient co-transport and dual incorporation of two different ncAAs.

Conclusions:

  • Engineering cellular uptake systems is a powerful strategy for enhancing genetic code expansion.
  • The developed approach enables programmable import of a wide range of chemically diverse building blocks.
  • This work significantly advances the capabilities of ncAA incorporation for basic research and biotechnology.