HO1 and PcyA proteins involved in phycobilin biosynthesis form a 1:2 complex with ferredoxin‐1 required for photosynthesis

Okada, Ken

doi:10.1016/j.febslet.2009.03.052

Cited by 20 publications

(23 citation statements)

References 23 publications

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“…We probed the proposed model directly as proposed in the literature and similar pathways published. 17 , 25 , 43 We complement this work showing the model’s agreement with the tested pathway, demonstrating how heme, Fd, and FNR are rate limiting factors for the production of PCB, as confirmed experimentally in Figures 1 , 2 and 3 . A full description of the kinetic model can be found in Supporting Information .…”

Section: Methodssupporting

confidence: 73%

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP⁺ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

et al. 2018

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Transplanting metabolic reactions from one species into another has many uses as a research tool with applications ranging from optogenetics to crop production. Ferredoxin (Fd), the enzyme that most often supplies electrons to these reactions, is often overlooked when transplanting enzymes from one species to another because most cells already contain endogenous Fd. However, we have shown that the production of chromophores used in Phytochrome B (PhyB) optogenetics is greatly enhanced in mammalian cells by expressing bacterial and plant Fds with ferredoxin-NADP+ reductases (FNR). We delineated the rate limiting factors and found that the main metabolic precursor, heme, was not the primary limiting factor for producing either the cyanobacterial or plant chromophores, phycocyanobilin or phytochromobilin, respectively. In fact, Fd is limiting, followed by Fd+FNR and finally heme. Using these findings, we optimized the PCB production system and combined it with a tissue penetrating red/far-red sensing PhyB optogenetic gene switch in animal cells. We further characterized this system in several mammalian cell lines using red and far-red light. Importantly, we found that the light-switchable gene system remains active for several hours upon illumination, even with a short light pulse, and requires very small amounts of light for maximal activation. Boosting chromophore production by matching metabolic pathways with specific ferredoxin systems will enable the unparalleled use of the many PhyB optogenetic tools and has broader implications for optimizing synthetic metabolic pathways.

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Section: Methodssupporting

confidence: 73%

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP⁺ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

et al. 2018

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“…However, the opening could also be protected by interaction with another protein, including the target apoprotein ( Fig. S4), but also the reductase, PcyA, that generates PCB from biliverdin and has been implied in substrate channeling (40,41). It is, furthermore, conceivable that the N-terminal arm of the E subunit swings over the opening of the cavity upon chromophore binding (see below).…”

Section: Significancementioning

confidence: 99%

Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F

Zhao

Höppner

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The light-harvesting phycobilisome in cyanobacteria and red algae requires the lyase-catalyzed chromophorylation of phycobiliproteins. There are three functionally distinct lyase families known. The heterodimeric E/F type is specific for attaching bilins covalently to α-subunits of phycocyanins and phycoerythrins. Unlike other lyases, the lyase also has chromophore-detaching activity. A subclass of the E/F-type lyases is, furthermore, capable of chemically modifying the chromophore. Although these enzymes were characterized >25 y ago, their structures remained unknown. We determined the crystal structure of the heterodimer of CpcE/F from sp. PCC7120 at 1.89-Å resolution. Both subunits are twisted, crescent-shaped α-solenoid structures. CpcE has 15 and CpcF 10 helices. The inner (concave) layer of CpcE (helices h2, 4, 6, 8, 10, 12, and 14) and the outer (convex) layer of CpcF (h16, 18, 20, 22, and 24) form a cavity into which the phycocyanobilin chromophore can be modeled. This location of the chromophore is supported by mutations at the interface between the subunits and within the cavity. The structure of a structurally related, isomerizing lyase, PecE/F, that converts phycocyanobilin into phycoviolobilin, was modeled using the CpcE/F structure as template. A HC motif critical for the isomerase activity of PecE/F is located at the loop between h20 and h21, supporting the proposal that the nucleophilic addition of Cys-88 to C10 of phycocyanobilin induces the isomerization of phycocyanobilin into phycoviolobilin. Also, the structure of NblB, involved in phycobilisome degradation could be modeled using CpcE as template. Combined with CpcF, NblB shows a low chromophore-detaching activity.

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“…nsp-Fd1 interacts with FNR and nitrate reductase (NIR) (44,45). te-Fd1 interacts with FNR, PSI, heme oxygenase (HO), PcyA, and 4-Hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) (46)(47)(48). This latter oxidoreductase is in the non-mevalonate pathway for isoprenoid biosynthesis (48).…”

Section: Cyanophage and Host Fds: Evolutionary Linksmentioning

confidence: 99%

Prochlorococcusphage ferredoxin: structural characterization and electron transfer to cyanobacterial sulfite reductases

Campbell

Olmos

et al. 2020

Preprint

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Marine cyanobacteria are infected by phage whose genomes encode ferredoxin (Fd) electron carriers. While these Fds are thought to redirect the energy harvested from light to phage-encoded oxidoreductases that enhance viral fitness, it is not clear how the biochemical and biophysical properties of phage Fds relate to those in photosynthetic organisms. Bioinformatic analysis using a sequence similarity network revealed that phage Fds are most closely related to cyanobacterial Fds that transfer electrons from photosystems to oxidoreductases involved in nutrient assimilation. Structural analysis of myovirus P-SSM2 Fd (pssm2-Fd), which infects Prochlorococcus marinus, revealed high similarity to cyanobacterial Fds (≤0.5 Å RMSD). Additionally, pssm2-Fd exhibits a low midpoint reduction potential (-336 mV vs. SHE) similar to other photosynthetic Fds, albeit lower thermostability (Tm = 28°C) than many Fds. When expressed in an Escherichia coli strain with a sulfite assimilation defect, pssm2-Fd complemented growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggests that phage Fds evolved to transfer electrons to both phage-and cyanobacterial-encoded oxidoreductases.

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HO1 and PcyA proteins involved in phycobilin biosynthesis form a 1:2 complex with ferredoxin‐1 required for photosynthesis

Cited by 20 publications

References 23 publications

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP⁺ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP⁺ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F

Prochlorococcusphage ferredoxin: structural characterization and electron transfer to cyanobacterial sulfite reductases

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HO1 and PcyA proteins involved in phycobilin biosynthesis form a 1:2 complex with ferredoxin‐1 required for photosynthesis

Cited by 20 publications

References 23 publications

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP+ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP+ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F

Prochlorococcusphage ferredoxin: structural characterization and electron transfer to cyanobacterial sulfite reductases

Contact Info

Product

Resources

About

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP⁺ Reductase Systems Enables Genetically Encoded PhyB Optogenetics

Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP⁺ Reductase Systems Enables Genetically Encoded PhyB Optogenetics