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

  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},
  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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A multiplasmid coexpression system was used to recreate the biosynthetic pathway for phycobiliproteins from the cyanobacterium Synechococcus sp.

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Cloning of pcB and pcA Gene from Gracilariopsis lemaneiformis and Expression of a Fluorescent Phycocyanin in Heterologous Host

This research provides a supplement for the comprehensive understanding of the assembly mechanism of optically active phycocyanin in red algae.

Phycourobilin in Trichromatic Phycocyanin from Oceanic Cyanobacteria Is Formed Post-translationally by a Phycoerythrobilin Lyase-Isomerase*

A unique trichromatic phycocyanin, R-PC V, extracted fromphycobilisomes of Synechococcus sp.

Phycocyanobilin:Ferredoxin Oxidoreductase ofAnabaena sp. PCC 7120

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.

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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A gene containing an open reading frame with a predicted polypeptide that has a sequence similar to that of a conserved region of animal microsomal heme oxygenases was identified in the published genomic sequence of Synechocystis sp.

Candidate genes for the phycoerythrocyanin alpha subunit lyase. Biochemical analysis of pecE and pecF interposon mutants.

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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Three new classes of bilin reductases with distinct substrate/product specificities that are involved in the biosynthesis of the phycobiliprotein chromophore precursors phycoerythrobilin andphycocyanobilin are defined.

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When two genes in the phycocyanin operon of this organism, cpcE and cpcF, are inactivated by insertion, together or separately, the surprising result is elimination of correct bilin attachment at only one site, that on the alpha subunit of phyCOCyanin.

Candidate Genes for the Phycoerythrocyanin α Subunit Lyase.

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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Recombinant phycobiliproteins. Recombinant C-phycocyanins equipped with affinity tags, oligomerization, and biospecific recognition domains.

The methods described here achieve in vivo production of stable oligomeric phycobiliprotein constructs equipped with affinity purification tags and biospecific recognition domains usable as fluorescent labels without further chemical manipulation.

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The spontaneous addition of PCB to PecA and that of the reaction catalyzed by PecE/F, were characterized by their photochemistry and by absorption, fluorescence, circular dichroism of the four states obtained by irradiation with light and/or modification of Cys-alpha 98/99 with thiol-directed reagents.