ArticlePhotosynthesis research2020
Far-red light allophycocyanin subunits play a role in chlorophyll d accumulation in far-red light.
Article in Photosynthesis research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Previously unrecognized diversity of far-red light-using terrestrial green algae and cyanobacteria.iScience · 2025Article
- The molecular basis of the most red-shifted allophycocyanin discovered to date.Photosynthesis research · 2025Article
- Structure of a stripped-down and tuned-up far-red phycobilisome.Communications biology · 2025Article
- Non-linear frequency-doubling up-conversion in sulfide minerals enables deep-sea oxygenic photosynthesis.National science review · 2025Article
- Far-red light-driven photoautotrophy of chlorophyll f-producing cyanobacterium without red-shifted phycobilisome core complex.Photosynthesis research · 2025Article
- Structural comparison of allophycocyanin variants reveals the molecular basis for their spectral differences.Photosynthesis research · 2024Article
- Crystallographic and biochemical analyses of a far-red allophycocyanin to address the mechanism of the super-red-shift.Photosynthesis research · 2024Article
- The structural basis for light harvesting in organisms producing phycobiliproteins.The Plant cell · 2024Review
- Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335.The Journal of biological chemistry · 2024Article
- Molecular diversity and evolution of far-red light-acclimated photosystem I.Frontiers in plant science · 2023Article
- Molecular Evolution of Far-Red Light-Acclimated Photosystem II.Microorganisms · 2022Article
- The antenna of far-red absorbing cyanobacteria increases both absorption and quantum efficiency of Photosystem II.Nature communications · 2022Article
- Adaptation of Cyanobacteria to the Endolithic Light Spectrum in Hyper-Arid Deserts.Microorganisms · 2022Article
- Changes in supramolecular organization of cyanobacterial thylakoid membrane complexes in response to far-red light photoacclimation.Science advances · 2022Article
- Structure of a photosystem I-ferredoxin complex from a marine cyanobacterium provides insights into far-red light photoacclimation.The Journal of biological chemistry · 2022Article
- The structural basis of far-red light absorbance by allophycocyanins.Photosynthesis research · 2021Article
- Global distribution of a chlorophyll f cyanobacterial marker.The ISME journal · 2020Article
- Characterization of cyanobacterial allophycocyanins absorbing far-red light.Photosynthesis research · 2020Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
Some terrestrial cyanobacteria acclimate to and utilize far-red light (FRL; λ = 700-800 nm) for oxygenic photosynthesis, a process known as far-red light photoacclimation (FaRLiP). A conserved, 20-gene FaRLiP cluster encodes core subunits of Photosystem I (PSI) and Photosystem II (PSII), five phycobiliprotein subunits of FRL-bicylindrical cores, and enzymes for synthesis of chlorophyll (Chl) f and possibly Chl d. Deletion mutants for each of the five apc genes of the FaRLiP cluster were constructed in Synechococcus sp. PCC 7335, and all had similar phenotypes. When the mutants were grown in white (WL) or red (RL) light, the cells closely resembled the wild-type (WT) strain grown under the same conditions. However, the WT and mutant strains were very different when grown under FRL. Mutants grown in FRL were unable to assemble FRL-bicylindrical cores, were essentially devoid of FRL-specific phycobiliproteins, but retained RL-type phycobilisomes and WL-PSII. The transcript levels for genes of the FaRLiP cluster in the mutants were similar to those in WT. Surprisingly, the Chl d contents of the mutant strains were greatly reduced (~ 60-99%) compared to WT and so were the levels of FRL-PSII. We infer that Chl d may be essential for the assembly of FRL-PSII, which does not accumulate to normal levels in the mutants. We further infer that the cysteine-rich subunits of FRL allophycocyanin may either directly participate in the synthesis of Chl d or that FRL bicylindrical cores stabilize FRL-PSII to prevent loss of Chl d.
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