ArticleNature microbiology2023
Plastid-localized xanthorhodopsin increases diatom biomass and ecosystem productivity in iron-limited surface oceans.
Article in Nature microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Evidence for the acquisition of a proteorhodopsin-like rhodopsin by a chrysophyte-infecting giant virus.Journal of virology · 2026Article
- Unexpected microbial rhodopsin dynamics in sync with phytoplankton blooms.Nature communications · 2025Article
- The Evolution of Southern Ocean Net Primary Production in a Changing Climate: Challenges and Opportunities.Global change biology · 2025Article
- Light-harvesting by antenna-containing xanthorhodopsin from an Antarctic Pseudanabaenaceae cyanobacterium.Communications biology · 2025Article
- Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genetic engineering in diatoms: advances and prospects.The Plant journal : for cell and molecular biology · 2025Review
- Survival strategies of planktonic organisms in alpine lakes and beyond: Baldi Memorial Award Lecture presented at the 37th Congress of the International Society of Limnology.Inland waters : journal of the International Society of Limnology · 2025Article
- Proton-pumping rhodopsins promote the growth and survival of phytoplankton in a highly variable ocean.The ISME journal · 2024Article
- Eukaryotic viruses encode the ribosomal protein eL40.Npj viruses · 2024Article
- Iron-limitation light switch.Nature microbiology · 2023Article
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 4 countries.
Funding
Abstract
Microbial rhodopsins are photoreceptor proteins that convert light into biological signals or energy. Proteins of the xanthorhodopsin family are common in eukaryotic photosynthetic plankton including diatoms. However, their biological role in these organisms remains elusive. Here we report on a xanthorhodopsin variant (FcR1) isolated from the polar diatom Fragilariopsis cylindrus. Applying a combination of biophysical, biochemical and reverse genetics approaches, we demonstrate that FcR1 is a plastid-localized proton pump which binds the chromophore retinal and is activated by green light. Enhanced growth of a Thalassiora pseudonana gain-of-function mutant expressing FcR1 under iron limitation shows that the xanthorhodopsin proton pump supports growth when chlorophyll-based photosynthesis is iron-limited. The abundance of xanthorhodopsin transcripts in natural diatom communities of the surface oceans is anticorrelated with the availability of dissolved iron. Thus, we propose that these proton pumps convey a fitness advantage in regions where phytoplankton growth is limited by the availability of dissolved iron.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.