Heterologous expression of cyanobacterial Orange Carotenoid Protein (OCP2) as a soluble carrier of ketocarotenoids in Chlamydomonas reinhardtii

Pivato, Matteo; Perozeni, Federico; Licausi, Francesco; Cazzaniga, Stefano; Ballottari, Matteo

doi:10.1016/j.algal.2021.102255

Cited by 16 publications

(15 citation statements)

References 66 publications

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“…Upon absorption of strong blue–green light, the noncovalently bound ketocarotenoid transfers from the CTD to the NTD, thereby undergoing a conformational change and a shift in color from orange to red, thus activating the quenching state. OCP has not only been expressed in ketocarotenoid‐producing microalgae for better solubilization of the ketocarotenoids canthaxanthin and astaxanthin for their use as nutraceuticals (Pivato et al, 2021), but is also being exploited as a possible photoswitchable protein in plants with implementations for plastid optogenetics, artificial photosynthesis and synthetic biology due to its light‐dependent conformational changes and uniqueness in cyanobacteria (Andreoni et al, 2017; Lechno‐Yossef et al, 2017; Dominguez‐Martin and Kerfeld, 2019; Piccinini et al, 2021).…”

Section: Improving Crop Yields Through Optimization Of Photosynthetic...mentioning

confidence: 99%

Here comes the sun: How optimization of photosynthetic light reactions can boost crop yields

Walter

Kromdijk

2022

JIPB

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Section: Improving Crop Yields Through Optimization Of Photosynthetic...mentioning

confidence: 99%

Here comes the sun: How optimization of photosynthetic light reactions can boost crop yields

Walter

Kromdijk

2022

JIPB

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“…It is known that a molecule of ketocarotenoid such as echinenone or 3hydroxyechinenone or canthaxanthin is required for OCP photoactivity, whereas ZEA binding does not render OCP photoactive [53]. A recent study has detected OCP photoactivity in the presence of a mixture of CAN and AXT [54]; however, the experimental settings used left the question of OCP photoactivity with exclusively AXT unresolved. We mixed the apoform of Synechocystis OCP with various AstaP-carotenoid complexes and analyzed the outcome of the potential protein-protein carotenoid transfer by ASESC.…”

Section: Carotenoid Proteinmentioning

confidence: 99%

Microalgal protein AstaP is a potent carotenoid solubilizer and delivery module with a broad carotenoid binding repertoire

Slonimskiy

Egorkin

Friedrich

et al. 2021

Preprint

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Carotenoids are lipophilic substances with many biological functions, from coloration to photoprotection. Being potent antioxidants, carotenoids have multiple biomedical applications, including the treatment of neurodegenerative disorders and retina degeneration. Nevertheless, the delivery of carotenoids is substantially limited by their poor solubility in the aqueous phase. Natural water-soluble carotenoproteins can facilitate this task, necessitating studies on their ability to uptake and deliver carotenoids. One such promising carotenoprotein, AstaP (Astaxanthin-binding protein), was recently identified in eukaryotic microalgae, but its structure and functional properties remained largely uncharacterized. By using a correctly folded recombinant protein, here we show that AstaP is an efficient carotenoid solubilizer that can stably bind not only astaxanthin but also zeaxanthin, canthaxanthin, and, to a lesser extent, β-carotene, i.e. carotenoids especially valuable to human health. AstaP accepts carotenoids provided as acetone solutions or embedded in membranes, forming carotenoid-protein complexes with an apparent stoichiometry of 1:1. We successfully produced AstaP holoproteins in specific carotenoid-producing strains of Escherichia coli, proving it is amenable to cost-efficient biotechnology processes. Regardless of the carotenoid type, AstaP remains monomeric in both apo- and holoforms, while its rather minimalistic mass (∼20 kDa) makes it an especially attractive antioxidant delivery module. In vitro, AstaP transfers different carotenoids to the liposomes and to unrelated proteins from cyanobacteria, which can modulate their photoactivity and/or oligomerization. These findings expand the toolkit of the characterized carotenoid-binding proteins and outline the perspective of the use of AstaP as a unique monomeric antioxidant nanocarrier with an extensive carotenoid-binding repertoire.

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“…It is known that a molecule of ketocarotenoid such as echinenone or 3‐hydroxyechinenone or canthaxanthin is required for OCP photoactivity, whereas ZEA binding does not render OCP photoactive [53]. A recent study has detected OCP photoactivity in the presence of a mixture of CAN and AXT [54]; however, the experimental settings used left the question of OCP photoactivity with exclusively AXT unresolved.…”

Section: Resultsmentioning

confidence: 99%

Microalgal protein AstaP is a potent carotenoid solubilizer and delivery module with a broad carotenoid binding repertoire

et al. 2021

View full text Add to dashboard Cite

Carotenoids are lipophilic substances with many biological functions, from coloration to photoprotection. Being potent antioxidants, carotenoids have multiple biomedical applications, including the treatment of neurodegenerative disorders and retina degeneration. Nevertheless, the delivery of carotenoids is substantially limited by their poor solubility in the aqueous phase. Natural water-soluble carotenoproteins can facilitate this task, necessitating studies on their ability to uptake and deliver carotenoids. One such promising carotenoprotein, AstaP (astaxanthin-binding protein), was recently identified in eukaryotic microalgae, but its structure and functional properties remained largely uncharacterized. By using a correctly folded recombinant protein, here we show that AstaP is an efficient carotenoid solubilizer that can stably bind not only astaxanthin but also zeaxanthin, canthaxanthin, and, to a lesser extent, b-carotene, that is, carotenoids especially valuable to human health. AstaP accepts carotenoids provided as acetone solutions or embedded in membranes, forming carotenoid-protein complexes with an apparent stoichiometry of 1:1. We successfully produced AstaP holoproteins in specific carotenoid-producing strains of Escherichia coli, proving it is amenable to cost-efficient biotechnology processes. Regardless of the carotenoid type, AstaP remains monomeric in both apo-and holoform, while its rather minimalistic mass (~20 kDa) makes it an especially attractive antioxidant delivery module. In vitro, AstaP transfers different carotenoids to liposomes and to unrelated proteins from cyanobacteria, which can modulate their photoactivity and/or oligomerization. These findings expand the toolkit of the characterized carotenoid binding proteins and outline the perspective of the use of AstaP as a unique monomeric antioxidant nanocarrier with an extensive carotenoid binding repertoire.

show abstract

Heterologous expression of cyanobacterial Orange Carotenoid Protein (OCP2) as a soluble carrier of ketocarotenoids in Chlamydomonas reinhardtii

Cited by 16 publications

References 66 publications

Here comes the sun: How optimization of photosynthetic light reactions can boost crop yields

Here comes the sun: How optimization of photosynthetic light reactions can boost crop yields

Microalgal protein AstaP is a potent carotenoid solubilizer and delivery module with a broad carotenoid binding repertoire

Microalgal protein AstaP is a potent carotenoid solubilizer and delivery module with a broad carotenoid binding repertoire

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