ArticleArchives of microbiology2026
Evolutionary diversification of polyketide synthase (PKS) enzymes in Monascus purpureus strains for exploitation as a molecular factory.
Article in Archives of microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.
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- Erratum issued
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Abstract
Monascus purpureus is a significant filamentous fungus that is frequently used to produce pigments and bioactive compounds. However, little is known about its capacity for polyketide biosynthesis. In this work, we used sequence similarity, domain architecture, KEGG mapping, protein interaction analysis, homology modelling, and domain-adjacency Jaccard similarity to conduct a thorough genome-scale analysis of polyketide synthases (PKSs) in M. purpureus. Eight polyketide synthases (PKSs) were identified and classified into three groups: hybrid PKS-NRPS, highly reducing PKSs, and non-reducing PKSs. Product prediction analyses indicated that the organism has the biosynthetic potential to produce a wide range of secondary metabolites, including pigments, mycotoxins, phytotoxins, and pharmaceutically relevant compounds. Specifically, these PKSs were linked to the putative biosynthesis of citrinin, mitorubrinol, melanin, fusarin, cornexistin, byssochlamic acid, and xenolozoyenone. Their participation in global secondary metabolism, statin-like biosynthesis, aromatic polyketide formation, indole diterpene pathways, and lipid-related metabolism was verified by KEGG pathway mapping. Strong clustering among highly reducing PKSs, conservation among non-reducing aromatic PKSs, and notable divergence of hybrid PKS-NRPS systems were all revealed by domain-adjacency similarity analysis, indicating domain gain, loss, and fusion are the main drivers of PKS diversification in M. purpureus, rather than internal domain shuffling.STRING network analysis indicated that PKSs function primarily as autonomous biosynthetic units regulated at the gene cluster level. Homology modelling further confirmed that all PKSs possess structurally coherent catalytic folds. Overall, M. purpureus exhibits a diverse, evolutionarily plastic PKS repertoire that fuels its chemical diversity and dual toxicological and biotechnological relevance.
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