ArticleApplied and environmental microbiology2010
Biosynthesis of cyanobacterial phycobiliproteins in Escherichia coli: chromophorylation efficiency and specificity of all bilin lyases from Synechococcus sp. strain PCC 7002.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 78 citations in OpenAlex.
- Improved Stability and Brightness Following Iterative Redesign of a De Novo Biliprotein.Biochemistry · 2026Article
- Heterologous Reconstitution of the Biosynthesis Pathway for Producing Holo-C-Phycocyanin Alpha Subunit (CpcA) from Thermosynechococcus sp. TUBT-T01.Molecular biotechnology · 2026Article
- Production and Applications of Cyanobacterial Phycocyanin: Trends and Prospects.Indian journal of microbiology · 2025Article
- Assembly of allophycocyanin from individual subunits: involvement of apo-form in the formation of trimers.Photosynthesis research · 2025Article
- Functional Modification of Cyanobacterial Phycobiliprotein and Phycobilisomes through Bilin Metabolism Control.ACS synthetic biology · 2024Article
- Recent Progress of Natural and Recombinant Phycobiliproteins as Fluorescent Probes.Marine drugs · 2023Review
- Loss of Biliverdin Reductase Increases Oxidative Stress in the CyanobacteriumMicroorganisms · 2023Article
- The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions.International journal of molecular sciences · 2023Review
- Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Allophycocyanin A is a carbon dioxide receptor in the cyanobacterial phycobilisome.Nature communications · 2022Article
- Acclimation of the photosynthetic apparatus to low light in a thermophilic Synechococcus sp. strain.Photosynthesis research · 2022Article
- Phycobiliproteins-A Family of Algae-Derived Biliproteins: Productions, Characterization and Pharmaceutical Potentials.Marine drugs · 2022Review
- Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives.Computational and structural biotechnology journal · 2022Review
- The phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Molecular bases of an alternative dual-enzyme system for light color acclimation of marineProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The structural basis of far-red light absorbance by allophycocyanins.Photosynthesis research · 2021Article
- Characterization of cyanobacterial allophycocyanins absorbing far-red light.Photosynthesis research · 2020Article
- Biosynthesis and characterization of a recombinant eukaryotic allophycocyanin using prokaryotic accessory enzymes.MicrobiologyOpen · 2020Article
- Cloning ofGenes · 2019Article
- Metabolic engineering of Escherichia coli for efficient biosynthesis of fluorescent phycobiliprotein.Microbial cell factories · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phycobiliproteins are water-soluble, light-harvesting proteins that are highly fluorescent due to linear tetrapyrrole chromophores, which makes them valuable as probes. Enzymes called bilin lyases usually attach these bilin chromophores to specific cysteine residues within the alpha and beta subunits via thioether linkages. A multiplasmid coexpression system was used to recreate the biosynthetic pathway for phycobiliproteins from the cyanobacterium Synechococcus sp. strain PCC 7002 in Escherichia coli. This system efficiently produced chromophorylated allophycocyanin (ApcA/ApcB) and alpha-phycocyanin with holoprotein yields ranging from 3 to 12 mg liter(-1) of culture. This heterologous expression system was used to demonstrate that the CpcS-I and CpcU proteins are both required to attach phycocyanobilin (PCB) to allophycocyanin subunits ApcD (alpha(AP-B)) and ApcF (beta(18)). The N-terminal, allophycocyanin-like domain of ApcE (L(CM)(99)) was produced in soluble form and was shown to have intrinsic bilin lyase activity. Lastly, this in vivo system was used to evaluate the efficiency of the bilin lyases for production of beta-phycocyanin.
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