Thylakoid Targeting Improves Stability of a Cytochrome P450 in the Cyanobacterium Synechocystis sp. PCC 6803
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High Resolution Image Download MS PowerPoint Slide Plants produce a large array of natural products of biotechnological interest. In many cases, these compounds are naturally produced at low titers and involve complex biosynthetic pathways, which often include cytochrome P450 enzymes. P450s are known to be difficult to express in traditional heterotrophic chassis. However, cyanobacteria have shown promise as a sustainable alternative for the heterologous expression of P450s and light-driven product biosynthesis. In this study, we explore strategies for improving plant P450 stability and membrane insertion in cyanobacteria. The widely used model cyanobacterium Synechocystis sp. PCC 6803 was chosen as the host, and the well-studied P450 CYP79A1 from the dhurrin pathway of Sorghum bicolor was chosen as the model enzyme. Combinations of the P450 fused with individual elements (e.g., signal peptide, transmembrane domain) or the full length cyanobacterial, thylakoid-localized, protein PetC1 were designed. All generated CYP79A1 variants led to oxime production. Our data show that strains producing CYP79A1 variants with elements of PetC1 improved thylakoid targeting. In addition, chlorophyll-normalized oxime levels increased, on average, up to 18 times compared to the unmodified CYP79A1. These findings offer promising strategies to improve heterologous P450 expression in cyanobacteria and can ultimately contribute to advancing light-driven biocatalysis in cyanobacterial chassis.
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Thylakoid anchoring can position heterologous proteins close to photosynthetic electron transport components, ferredoxin and NADPH-generating systems, and this approach has been shown to improve the stability and activity of a heterologous cytochrome P450 in Synechocystis sp. PCC 6803.
“For membrane-associated or electron-transfer-dependent enzymes, thylakoid anchoring can position heterologous proteins close to photosynthetic electron transport components, ferredoxin and NADPH-generating systems. This approach has recently been shown to improve the stability and activity of a heterologous cytochrome P450 in Synechocystis sp. PCC 6803 [168].”
From Cyanobacteria as a Photosynthetic Chassis for Metabolic Pathway Engineering with Heterologous Gene Expression (2026) · cites this paper as [168]
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“This approach has recently been shown to improve the stability and activity of a heterologous cytochrome P450 in Synechocystis sp. PCC 6803 [168].”
- Authors
- Hanamghar, S. S., Mellor, S. B., Mikkelsen, L., Crocoll, C., Motawie, M. S., Russo, D. A., Jensen, P. E., & Zedler, J. A. Z.
- Affiliations
- Friedrich Schiller University Jena (DE)
- University of Copenhagen (DK)
- Department of Plant and Environmental Sciences
- Corresponding author
- Zedler, Julie A. Z.
- ORCID
- Venue
- ACS Synthetic Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2025-03-02
- Volume
- 14
- Issue
- 3
- Pages
- 867-877
- ISSN
- 2161-5063 (ISSN-L)
- PMC
- PMC11934225
- OpenAlex
- W4408085444
- Cited by
- 9
- References
- 74
- Citations by year
- 2026: 7 · 2025: 2
- FWCI
- 2.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- ACS Synthetic Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
- Common Library Network (Der Gemeinsame Bibliotheksverbund) (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (239748522)
- Novo Nordisk Fonden (NNF19OC0057634)
- H2020 Marie Sklodowska-Curie Actions (745959)
- Carlsbergfondet (CF17-0657)
- Alexander von Humboldt-Stiftung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Keywords
- cytochrome P450, Synechocystis sp. PCC 6803, sorghum, membrane insertion, protein stability, heterologous expression, signal peptide, transmembrane domain
- MeSH terms
- Bacterial Proteins, Cytochrome P-450 Enzyme System, Nitriles, Oximes, Thylakoids, Sorghum, Synechocystis
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