ArticleFrontiers in microbiology2015
RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP).
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Mapping the absorption landscape of far-red Photosystem II.Nature communications · 2026Article
- Transcriptomic Remodeling of Light Harvesting and Photosystem Genes inPlants (Basel, Switzerland) · 2026Article
- Low PSI content broadens the optimal light spectrum for a phycoerythrin-dominated cyanobacterium towards near far-red.Scientific reports · 2026Article
- Thylakoids reorganization enables driving photosynthesis under far-red light in the microalga Nannochloropsis gaditana.The New phytologist · 2026Article
- Driving Electron Transfer in Photosystem I Using Far-Red Light: Overall Perspectives.Plants (Basel, Switzerland) · 2025Review
- 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
- Far-red light-driven photoautotrophy of chlorophyll f-producing cyanobacterium without red-shifted phycobilisome core complex.Photosynthesis research · 2025Article
- Article
- Crystallographic and biochemical analyses of a far-red allophycocyanin to address the mechanism of the super-red-shift.Photosynthesis research · 2024Article
- Cyanobacteriochromes: A Rainbow of Photoreceptors.Annual review of microbiology · 2024Review
- The structural basis for light harvesting in organisms producing phycobiliproteins.The Plant cell · 2024Review
- Two cyanobacterial species exhibit stress responses when grown together in visible light or far-red light.mSphere · 2024Article
- Photosystem I: A Paradigm for Understanding Biological Environmental Adaptation Mechanisms in Cyanobacteria and Algae.International journal of molecular sciences · 2024Review
- Snapshots of the Reaction Coordinate of a Thermophilic 2'-Deoxyribonucleoside/ribonucleoside Transferase.ACS catalysis · 2024Article
- Cyanobacteriochromes from Gloeobacterales Provide New Insight into the Diversification of Cyanobacterial Photoreceptors.Journal of molecular biology · 2024Article
- Far-red light photoacclimation in a desertFrontiers in microbiology · 2024Article
- Responding to light signals: a comprehensive update on photomorphogenesis in cyanobacteria.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Review
- Identification of a Far-Red Light-Inducible Promoter that Exhibits Light Intensity Dependency and Reversibility in a Cyanobacterium.ACS synthetic biology · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terrestrial cyanobacteria often occur in niches that are strongly enriched in far-red light (FRL; λ > 700 nm). Some cyanobacteria exhibit a complex and extensive photoacclimation response, known as FRL photoacclimation (FaRLiP). During the FaRLiP response, specialized paralogous proteins replace 17 core subunits of the three major photosynthetic complexes: Photosystem (PS) I, PS II, and the phycobilisome. Additionally, the cells synthesize both chlorophyll (Chl) f and Chl d. Using biparental mating from Escherichia coli, we constructed null mutants of three genes, rfpA, rfpB, and rfpC, in the cyanobacteria Chlorogloeopsis fritschii PCC 9212 and Chroococcidiopsis thermalis PCC 7203. The resulting mutants were no longer able to modify their photosynthetic apparatus to absorb FRL, were no longer able to synthesize Chl f, inappropriately synthesized Chl d in white light, and were unable to transcribe genes of the FaRLiP gene cluster. We conclude that RfpA, RfpB, and RfpC constitute a FRL-activated signal transduction cascade that is the master control switch for the FaRLiP response. FRL is proposed to activate (or inactivate) the histidine kinase activity of RfpA, which leads to formation of the active state of RfpB, the key response regulator and transcription activator. RfpC may act as a phosphate shuttle between RfpA and RfpB. Our results show that reverse genetics via conjugation will be a powerful approach in detailed studies of the FaRLiP response.
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