ArticleJournal of bacteriology2011
Effects of modified Phycobilin biosynthesis in the Cyanobacterium Synechococcus sp. Strain PCC 7002.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- Evolutionary insights into bilin biosynthesis: Functional characterization of pre-PcyA enzymes.Protein science : a publication of the Protein Society · 2026Article
- Comparative study of phycoerythrobilin synthases for fine-tuning photosynthetic light-harvesting complexes, phycobilisomes.Scientific reports · 2026Article
- Archaean green-light environments drove the evolution of cyanobacteria's light-harvesting system.Nature ecology & evolution · 2025Article
- Systems metabolic engineering ofFrontiers in plant science · 2025Article
- Functional Modification of Cyanobacterial Phycobiliprotein and Phycobilisomes through Bilin Metabolism Control.ACS synthetic biology · 2024Article
- The Impact of Viral Infection on the Chemistries of the Earth's Most Abundant Photosynthesizes: Metabolically Talented Aquatic Cyanobacteria.Biomolecules · 2023Article
- GUN4 appeared early in cyanobacterial evolution.PNAS nexus · 2023Article
- Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Production of thermostable phycocyanin in a mesophilic cyanobacterium.Metabolic engineering communications · 2021Article
- Rapid analytical methods for the microalgal and cyanobacterial biorefinery: Application on strains of industrial importance.MicrobiologyOpen · 2021Article
- A far-red cyanobacteriochrome lineage specific for verdins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Characterization of Ferredoxin-Dependent Biliverdin Reductase PCYA1 Reveals the Dual Function in Retrograde Bilin Biosynthesis and Interaction With Light-Dependent Protochlorophyllide Oxidoreductase LPOR inFrontiers in plant science · 2018Article
- Algal light sensing and photoacclimation in aquatic environments.Plant, cell & environment · 2017Review
- Ferredoxin-dependent bilin reductases in eukaryotic algae: Ubiquity and diversity.Journal of plant physiology · 2017Article
- Streamlining recombination-mediated genetic engineering by validating three neutral integration sites inJournal of biological engineering · 2017Article
- CRISPR interference as a titratable, trans-acting regulatory tool for metabolic engineering in the cyanobacterium Synechococcus sp. strain PCC 7002.Metabolic engineering · 2016Article
- Lauric Acid Production in a Glycogen-Less Strain of Synechococcus sp. PCC 7002.Frontiers in bioengineering and biotechnology · 2015Article
- ChlR protein of Synechococcus sp. PCC 7002 is a transcription activator that uses an oxygen-sensitive [4Fe-4S] cluster to control genes involved in pigment biosynthesis.The Journal of biological chemistry · 2014Article
- Phycobilisome-Deficient Strains of Synechocystis sp. PCC 6803 Have Reduced Size and Require Carbon-Limiting Conditions to Exhibit Enhanced Productivity.Plant physiology · 2014Article
- Structural and biochemical characterization of the bilin lyase CpcS from Thermosynechococcus elongatus.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pathway for phycocyanobilin biosynthesis in Synechococcus sp. strain PCC 7002 comprises two enzymes: heme oxygenase and phycocyanobilin synthase (PcyA). The phycobilin content of cells can be modified by overexpressing genes encoding alternative enzymes for biliverdin reduction. Overexpression of the pebAB and HY2 genes, encoding alternative ferredoxin-dependent biliverdin reductases, caused unique effects due to the overproduction of phycoerythrobilin and phytochromobilin, respectively. Colonies overexpressing pebAB became reddish brown and visually resembled strains that naturally produce phycoerythrin. This was almost exclusively due to the replacement of phycocyanobilin by phycoerythrobilin on the phycocyanin α-subunit. This phenotype was unstable, and such strains rapidly reverted to the wild-type appearance, presumably due to strong selective pressure to inactivate pebAB expression. Overproduction of phytochromobilin, synthesized by the Arabidopsis thaliana HY2 product, was tolerated much better. Cells overexpressing HY2 were only slightly less pigmented and blue-green than the wild type. Although the pcyA gene could not be inactivated in the wild type, pcyA was easily inactivated when cells expressed HY2. These results indicate that phytochromobilin can functionally substitute for phycocyanobilin in Synechococcus sp. strain PCC 7002. Although functional phycobilisomes were assembled in this strain, the overall phycobiliprotein content of cells was lower, the efficiency of energy transfer by these phycobilisomes was lower than for wild-type phycobilisomes, and the absorption cross-section of the cells was reduced relative to that of the wild type because of an increased spectral overlap of the modified phycobiliproteins with chlorophyll a. As a result, the strain producing phycobiliproteins carrying phytochromobilin grew much more slowly at low light intensity.
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