Three Redundant Synthetases Secure Redox-Active Pigment Production in the Basidiomycete Paxillus involutus.

Jana Braesel, Sebastian Götze, Firoz Shah, Daniel Heine, James Tauber, Christian Hertweck, Anders Tunlid, Pierre Stallforth, Dirk Hoffmeister

Research output: Contribution to journalArticlepeer-review

Abstract

The symbiotic fungus Paxillus involutus serves a critical role in maintaining forest ecosystems, which are carbon sinks of global importance. P. involutus produces involutin and other 2,5-diarylcyclopentenone pigments that presumably assist in the oxidative degradation of lignocellulose via Fenton chemistry. Their precise biosynthetic pathways, however, remain obscure. Using a combination of biochemical, genetic, and transcriptomic analyses, in addition to stable-isotope labeling with synthetic precursors, we show that atromentin is the key intermediate. Atromentin is made by tridomain synthetases of high similarity: InvA1, InvA2, and InvA5. An inactive atromentin synthetase, InvA3, gained activity after a domain swap that replaced its native thioesterase domain with that of InvA5. The found degree of multiplex biosynthetic capacity is unprecedented with fungi, and highlights the great importance of the metabolite for the producer.
Original languageEnglish
Pages (from-to)1325-1334
JournalChemistry and Biology
Volume22
Issue number10
DOIs
Publication statusPublished - 2015

Subject classification (UKÄ)

  • Microbiology
  • Forest Science

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