ArticleProceedings of the National Academy of Sciences of the United States of America2012
Phycoerythrin-specific bilin lyase-isomerase controls blue-green chromatic acclimation in marine Synechococcus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 80 citations in OpenAlex.
- Phycocyanobilin biosynthesis in Galdieria sulphuraria requires isomerization of phycoerythrobilin synthesized by bilin reductases.The FEBS journal · 2026Article
- Phytoplankton With Flexible Pigment Content Disadvantaged by Projected Future Decrease in Variability of the Ocean Light Spectrum.Global change biology · 2026Article
- Competition for light color between marineApplied and environmental microbiology · 2025Article
- Engineering of Phycourobilin Synthase: PubS to a Two-Electron Reductase.Plant & cell physiology · 2025Article
- Chromatic acclimation shapes phytoplankton biogeography.Science advances · 2025Article
- Functional Modification of Cyanobacterial Phycobiliprotein and Phycobilisomes through Bilin Metabolism Control.ACS synthetic biology · 2024Article
- Double-duty isomerases: a case study of isomerization-coupled enzymatic catalysis.Trends in biochemical sciences · 2024Review
- Differential acclimation kinetics of the two forms of type IV chromatic acclimaters occurring in marineFrontiers in microbiology · 2024Article
- Reflections on Cyanobacterial Chromatic Acclimation: Exploring the Molecular Bases of Organismal Acclimation and Motivation for Rethinking the Promotion of Equity in STEM.Microbiology and molecular biology reviews : MMBR · 2022Review
- Article
- A hybrid type of chromatic acclimation regulated by the dual green/red photosensory systems in cyanobacteria.Plant physiology · 2022Article
- Chromatic Acclimation Processes and Their Relationships with Phycobiliprotein Complexes.Microorganisms · 2022Article
- Phycobiliproteins-A Family of Algae-Derived Biliproteins: Productions, Characterization and Pharmaceutical Potentials.Marine drugs · 2022Review
- Diversity and Evolution of Pigment Types in Marine Synechococcus Cyanobacteria.Genome biology and evolution · 2022Article
- Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.Structure (London, England : 1993) · 2022Article
- Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae.ACS central science · 2022Article
- The phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Light quality, oxygenic photosynthesis and more.Photosynthetica · 2022Review
- 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
- Characterization of cyanobacterial allophycocyanins absorbing far-red light.Photosynthesis research · 2020Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The marine cyanobacterium Synechococcus is the second most abundant phytoplanktonic organism in the world's oceans. The ubiquity of this genus is in large part due to its use of a diverse set of photosynthetic light-harvesting pigments called phycobiliproteins, which allow it to efficiently exploit a wide range of light colors. Here we uncover a pivotal molecular mechanism underpinning a widespread response among marine Synechococcus cells known as "type IV chromatic acclimation" (CA4). During this process, the pigmentation of the two main phycobiliproteins of this organism, phycoerythrins I and II, is reversibly modified to match changes in the ambient light color so as to maximize photon capture for photosynthesis. CA4 involves the replacement of three molecules of the green light-absorbing chromophore phycoerythrobilin with an equivalent number of the blue light-absorbing chromophore phycourobilin when cells are shifted from green to blue light, and the reverse after a shift from blue to green light. We have identified and characterized MpeZ, an enzyme critical for CA4 in marine Synechococcus. MpeZ attaches phycoerythrobilin to cysteine-83 of the α-subunit of phycoerythrin II and isomerizes it to phycourobilin. mpeZ RNA is six times more abundant in blue light, suggesting that its proper regulation is critical for CA4. Furthermore, mpeZ mutants fail to normally acclimate in blue light. These findings provide insights into the molecular mechanisms controlling an ecologically important photosynthetic process and identify a unique class of phycoerythrin lyase/isomerases, which will further expand the already widespread use of phycoerythrin in biotechnology and cell biology applications.
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