4.8 Article

Changes in supramolecular organization of cyanobacterial thylakoid membrane complexes in response to far-red light photoacclimation

Journal

SCIENCE ADVANCES
Volume 8, Issue 6, Pages -

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abj4437

Keywords

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Funding

  1. Deutsche Forschungsgemeinschaft [NU 421/1]
  2. Royal Society University Research Fellowship [URF\R1\191548]
  3. Biotechnology and Biological Sciences Research Council [BB/M012166/1, BB/L011506/1, BB/R001383/1, BB/V002015/1, BB/V006630/1, BB/M000265/1]
  4. Leverhulme Trust [RPG-2019-045]
  5. U.S. National Science Foundation [MCB-1613022]
  6. Photosynthetic Antenna Research Center (PARC)
  7. Energy Frontier Research Center - DOE, Office of Science, Office of Basic Energy Sciences [DE-SC 0001035]
  8. European Research Council [854126]

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Cyanobacteria have developed strategies to adapt to different environments and utilize various strategies for photosynthesis. The study characterizes the molecular changes involved in FaRLiP and the supramolecular organization of photosystem I under FRL light, showing altered cellular distribution.
Cyanobacteria are ubiquitous in nature and have developed numerous strategies that allow them to live in a diverse range of environments. Certain cyanobacteria synthesize chlorophylls d and f to acclimate to niches enriched in far-red light (FRL) and incorporate paralogous photosynthetic proteins into their photosynthetic apparatus in a process called FRL-induced photoacclimation (FaRLiP). We characterized the macromolecular changes involved in FRL-driven photosynthesis and used atomic force microscopy to examine the supramolecular organization of photosystem I associated with FaRLiP in three cyanobacterial species. Mass spectrometry showed the changes in the proteome of Chroococcidiopsis thermalis PCC 7203 that accompany FaRLiP. Fluorescence lifetime imaging microscopy and electron microscopy reveal an altered cellular distribution of photosystem complexes and illustrate the cell-to-cell variability of the FaRLiP response.

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