TY - JOUR
T1 - First-class – biosynthesis of 6-MSA and bostrycoidin type I polyketides in Yarrowia lipolytica
AU - Bejenari, Mihaela
AU - Spedtsberg, Eva Mie Lang
AU - Mathiesen, Julie
AU - Jeppesen, Alexandra Claire
AU - Cernat, Lucia
AU - Toussaint, Aouregane
AU - Apostol, Cristina
AU - Stoianov, Victor
AU - Pedersen, Tobias Bruun
AU - Nielsen, Mikkel Rank
AU - Sørensen, Jens Laurids
N1 - Publisher Copyright:
Copyright © 2024 Bejenari, Spedtsberg, Mathiesen, Jeppesen, Cernat, Toussaint, Apostol, Stoianov, Pedersen, Nielsen and Sørensen.
PY - 2024
Y1 - 2024
N2 - Fungal polyketides are a large group of secondary metabolites, valuable due to their diverse spectrum of pharmacological activities. Polyketide biosynthesis in filamentous fungi presents some challenges: small yield and low-purity titers. To tackle these issues, we switched to the yeast Yarrowia lipolytica, an easily cultivable heterologous host. As an oleaginous yeast, Y. lipolytica displays a high flux of acetyl- and malonyl-CoA precursors used in lipid synthesis. Likewise, acetyl- and malonyl-CoA are the building blocks of many natural polyketides, and we explored the possibility of redirecting this flux toward polyketide production. Despite its promising prospect, Y. lipolytica has so far only been used for heterologous expression of simple type III polyketide synthases (PKSs) from plants. Therefore, we decided to evaluate the potential of Y. lipolytica by targeting the more complex fungal polyketides synthesized by type I PKSs. We employed a CRISPR-Cas9-mediated genome editing method to achieve markerless gene integration of the genes responsible for bostrycoidin biosynthesis in Fusarium solani (fsr1, fsr2, and fsr3) and 6-methylsalicylic acid (6-MSA) biosynthesis in Aspergillus hancockii (6MSAS). Moreover, we attempted titer optimization through metabolic engineering by overexpressing two enzymes, TGL4 and AOX2, involved in lipid β-oxidation, but we did not observe an effect on polyketide production. With maximum titers of 403 mg/L 6-MSA and 35 mg/L bostrycoidin, the latter being substantially higher than our previous results in Saccharomyces cerevisiae (2.2 mg/L), this work demonstrates the potential of Y. lipolytica as a platform for heterologous production of complex fungal polyketides.
AB - Fungal polyketides are a large group of secondary metabolites, valuable due to their diverse spectrum of pharmacological activities. Polyketide biosynthesis in filamentous fungi presents some challenges: small yield and low-purity titers. To tackle these issues, we switched to the yeast Yarrowia lipolytica, an easily cultivable heterologous host. As an oleaginous yeast, Y. lipolytica displays a high flux of acetyl- and malonyl-CoA precursors used in lipid synthesis. Likewise, acetyl- and malonyl-CoA are the building blocks of many natural polyketides, and we explored the possibility of redirecting this flux toward polyketide production. Despite its promising prospect, Y. lipolytica has so far only been used for heterologous expression of simple type III polyketide synthases (PKSs) from plants. Therefore, we decided to evaluate the potential of Y. lipolytica by targeting the more complex fungal polyketides synthesized by type I PKSs. We employed a CRISPR-Cas9-mediated genome editing method to achieve markerless gene integration of the genes responsible for bostrycoidin biosynthesis in Fusarium solani (fsr1, fsr2, and fsr3) and 6-methylsalicylic acid (6-MSA) biosynthesis in Aspergillus hancockii (6MSAS). Moreover, we attempted titer optimization through metabolic engineering by overexpressing two enzymes, TGL4 and AOX2, involved in lipid β-oxidation, but we did not observe an effect on polyketide production. With maximum titers of 403 mg/L 6-MSA and 35 mg/L bostrycoidin, the latter being substantially higher than our previous results in Saccharomyces cerevisiae (2.2 mg/L), this work demonstrates the potential of Y. lipolytica as a platform for heterologous production of complex fungal polyketides.
KW - 6-MSA
KW - Fusarium
KW - fusarubin
KW - heterologous production
KW - pigment
KW - polyketide synthase (PKS)
KW - Yarrowia lipolytica
KW - yeast
UR - http://www.scopus.com/inward/record.url?scp=85189607126&partnerID=8YFLogxK
U2 - 10.3389/ffunb.2024.1327777
DO - 10.3389/ffunb.2024.1327777
M3 - Journal article
AN - SCOPUS:85189607126
SN - 2673-6128
VL - 5
JO - Frontiers in Fungal Biology
JF - Frontiers in Fungal Biology
M1 - 1327777
ER -