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

  title={Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli.},
  author={Richard M. Alvey and Avijit Biswas and Wendy M. Schluchter and Donald A. Bryant},
  volume={50 22},
Many cyanobacteria use brilliantly pigmented, multisubunit macromolecular structures known as phycobilisomes as antenna to enhance light harvesting for photosynthesis. Recent studies have defined the enzymes that synthesize phycobilin chromophores as well as many of the phycobilin lyase enzymes that attach these chromophores to their cognate apoproteins. The ability of the phycocyanin α-subunit (CpcA) to bind alternative linear tetrapyrrole chromophores was examined through the use of a… 

Biosynthesis of a Phycocyanin Beta Subunit with Two Noncognate Chromophores in Escherichia coli

There are interactions between chromophores of CpcB which possibly together with the help of lyases lead to isomerization of PEB-Cys155-CpcB to PUB-Cycocyanin beta subunit, which can be used as fluorescent label in immunofluorescence assay.

Chromophorylation (in Escherichia coli) of allophycocyanin B subunits from far-red light acclimated Chroococcidiopsis thermalis sp. PCC7203.

  • Qianzhao XuQi-Ying Tang K. Zhao
  • Biology, Chemistry
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2017
This work studied the chromophorylation of the three far-red induced ApcD subunits Ap cD2, apcD3 andApcD4 from Chroococcidiopsis thermalis during the expression in E. coli, finding a red-shifted product carrying non-covalently bound phycocyanobilin could be detected in the supernatant after cell lysis.

Characterization of the Activities of the CpeY, CpeZ, and CpeS Bilin Lyases in Phycoerythrin Biosynthesis in Fremyella diplosiphon Strain UTEX 481*

When grown in green light, Fremyella diplosiphon strain UTEX 481 produces the red-colored protein phycoerythrin (PE) to maximize photosynthetic light harvesting. PE is composed of two subunits, CpeA

Structural and biochemical characterization of the bilin lyase CpcS from Thermosynechococcus elongatus.

The crystal structure of a bilin lyase of the CpcS family from Thermosynechococcus elongatus (TeCpcS-III), a 10-stranded β barrel with two alpha helices and belongs to the lipocalin structural family, is reported here.

Modular generation of fluorescent phycobiliproteins.

This approach facilitates chromophorylation studies of phycobiliproteins, as well as their use for fluorescence labeling based on their high fluorescence.

Production of thermostable phycocyanin in a mesophilic cyanobacterium

Metabolic engineering of Escherichia coli for efficient biosynthesis of fluorescent phycobiliprotein

This work demonstrated strategies for improving the chromophorylation of recombinant protein, especially biliprotein with heme, or its derivatives as a prosthetic group.

Phycoviolobilin formation and spectral tuning in the DXCF cyanobacteriochrome subfamily.

The ability of this subfamily to form PVB or retain PCB provides a powerful mechanism for tuning the photoproduct absorbance, with blue-absorbing dark states leading to a broad range of photobacteriochromes absorbing teal, green, yellow, or orange light.



Biosynthesis of Cyanobacterial Phycobiliproteins in Escherichia coli: Chromophorylation Efficiency and Specificity of All Bilin Lyases from Synechococcus sp. Strain PCC 7002

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

Chromophore attachment to phycobiliprotein beta-subunits: phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena Sp. PCC7120.

The gene alr0617, from the cyanobacterium Anabaena sp. PCC7120, which is homologous to cpeS from Gloeobacter violaceus PCC 7421, Fremyella diplosiphon (Calothrix PCC7601), and Synechococcus sp.

Effects of Modified Phycobilin Biosynthesis in the Cyanobacterium Synechococcus sp. Strain PCC 7002

Results indicate that phytochromobilin can functionally substitute for phycocyanobilin in Synechococcus sp.

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.

Phycobiliprotein biosynthesis in cyanobacteria: structure and function of enzymes involved in post-translational modification.

Several new families of bilin lyases are identified and characterized, which are responsible for attaching PCB to phycobiliproteins as well as the Asn methyl transferase for beta-subunits in Synechococcus sp.

Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins

  • K. ZhaoP. Su H. Scheer
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences
  • 2007
Using a modular multiplasmidic expression-reconstitution assay in Escherichia coli with low background binding, phycobilin:cystein-84 biliprotein lyase (CpeS1) from Anabaena PCC7120, has been characterized as a nearly universal lyase for the cysteine-84-binding site that is conserved in all biliproteins.

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

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

Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-alpha 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.

Phycocyanin alpha-subunit phycocyanobilin lyase.

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.