Biosynthesis of the Cyanobacterial Light-Harvesting Polypeptide Phycoerythrocyanin Holo-α Subunit in a Heterologous Host

@article{Tooley2002BiosynthesisOT,
  title={Biosynthesis of the Cyanobacterial Light-Harvesting Polypeptide Phycoerythrocyanin Holo-$\alpha$ Subunit in a Heterologous Host},
  author={Aaron J. Tooley and Alexander N. Glazer},
  journal={Journal of Bacteriology},
  year={2002},
  volume={184},
  pages={4666 - 4671}
}
ABSTRACT The entire pathway for the biosynthesis of the phycobiliviolin-bearing His-tagged holo-α subunit of the cyanobacterial photosynthetic accessory protein phycoerythrocyanin was reconstituted in Escherichia coli. Cyanobacterial genes encoding enzymes required for the conversion of heme to 3Z-phycocyanobilin, a precursor of phycobiliviolin (namely, heme oxygenase 1 and 3Z-phycocyanobilin:ferredoxin oxidoreductase), were expressed from a plasmid under the control of the hybrid trp-lac (trc… 
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59 Citations

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A radical mechanism for biliverdin IXα reduction by phycocyanobilin:ferredoxin oxidoreductase is envisaged, based on observations and the apparent lack of a metal or small molecule cofactor.

Gene Manipulation and Biosynthesis of Phycobiliproteins

Nonpigmented linker polypeptides are embedded in the structure which are responsible for stabilization and modulation of energy absorption within PBPs and help in effective energy transfers toward the photosystem.

Lyase activities of heterologous CpcS and CpcT for phycocyanin holo-β-subunit from Arthrospira platensis in Escherichia coli

CpcB was successfully synthesized in E. coli, to which co-expressed PCBs attached though at a relatively low efficiency, and the results showed that the attachment of PCBs to CpcB were carried out mainly by co-Expressed CpcS/U but CPCB also showed some autocatalytic activity.

Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli.

The ability of the phycocyanin α-subunit (CpcA) to bind alternative linear tetrapyrrole chromophores was examined through the use of a heterologous expression system in Escherichia coli and the recombinant proteins had unexpected and potentially useful properties.
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22 References

Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-α subunit in a heterologous host

The entire pathway for the synthesis of a fluorescent holophycobiliprotein subunit from a photosynthetic cyanobacterium was reconstituted in Escherichia coli, demonstrating the feasibility of generating constructs of these proteins in situ for use as fluorescent protein probes in living cells.

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The rod substructures of the Anabaena sp. PCC 7120 phycobilisome contain the light harvesting proteins C-phycocyanin and phycoerythrocyanin (PEC). Even at low light intensities, PEC represents no…

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The rod substructures of the Anabaena sp. PCC 7120 phycobilisome contain the light harvesting proteins C-phycocyanin and phycoerythrocyanin (PEC). Even at low light intensities, PEC represents no…

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