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Engineering a Fungal Non-Reducing Polyketide Synthase with an Apparently Inactive Product-Template Domain Reveals

Ruya Yin1, Yifei Qin1, Xingrui Liang1

  • 1State Key Laboratory of Agricultural and Forestry Biosecurity, MARA Key Lab of Pest Monitoring and Green Management, College of Plant Protection, China Agricultural University, Beijing 100193, China.

International Journal of Molecular Sciences
|June 26, 2026
PubMed
Summary

The product template (PT) domain in fungal non-reducing polyketide synthases (NR-PKS), even when seemingly inactive, influences product yield. Engineering the C-methyltransferase (CMT) domain of SorB halts polyketide production, indicating its crucial role.

Keywords:
C-methyltransferasebiosynthesiscatalytic reprogrammingdomain engineeringpolyketidepolyketide synthaseproduct templatesorbicillinsynthetic biology

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Mycology

Background:

  • Fungal iterative non-reducing polyketide synthases (NR-PKS) possess a product template (PT) domain crucial for aromatic cyclization.
  • Some NR-PKSs, like sorbicillin NR-PKS (SorB), feature a PT domain with unclear function.

Purpose of the Study:

  • To investigate the role of the PT domain in SorB's NR-PKS programming.
  • To explore the impact of engineering the PT and C-methyltransferase (CMT) domains on polyketide production.

Main Methods:

  • Dissection and engineering of the PT domain in SorB.
  • Phylogenetic tree analysis and multiple sequence alignments of PT domains.
  • Site-directed mutagenesis of the CMT domain's substrate-binding sites.

Main Results:

  • PT domain removal decreased product yield and lowered ketoacyl synthase (KS) domain transcription.
  • Mutations at catalytic dyad sites of the PT domain did not restore functionality.
  • Removal or site-directed mutation of the CMT domain abolished polyketide production.

Conclusions:

  • The PT domain, even if seemingly inactive, plays a role in NR-PKS yield and KS domain expression.
  • The CMT domain is essential for polyketide production and is susceptible to engineering in SorB.
  • Findings offer insights into the catalytic reprogramming of fungal NR-PKS.