Supramolecular organization of phycobiliproteins in the chlorophyll d-containing cyanobacterium Acaryochloris marina

FEBS Lett. 2009 Aug 6;583(15):2535-9. doi: 10.1016/j.febslet.2009.07.012. Epub 2009 Jul 15.

Abstract

Here we report the high-resolution detail of the organization of phycobiliprotein structures associated with photosynthetic membranes of the chlorophyll d-containing cyanobacterium Acaryochloris marina. Cryo-electron transmission-microscopy on native cell sections show extensive patches of near-crystalline phycobiliprotein rods that are associated with the stromal side of photosynthetic membranes. This supramolecular photosynthetic structure represents a novel mechanism of organizing the photosynthetic light-harvesting machinery. In addition, the specific location of phycobiliprotein patches suggests a physical separation of photosystem I and photosystem II reaction centres. Based on this finding and the known photosystem's structure in Acaryochloris, we discuss possible membrane arrangements of photosynthetic membrane complexes in this species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Chlorophyll / chemistry*
  • Chlorophyll / metabolism
  • Cyanobacteria / chemistry*
  • Cyanobacteria / metabolism
  • Cyanobacteria / ultrastructure
  • Models, Molecular
  • Photosynthesis / physiology
  • Photosynthetic Reaction Center Complex Proteins / chemistry
  • Photosynthetic Reaction Center Complex Proteins / metabolism
  • Phycobiliproteins / chemistry*
  • Phycobiliproteins / metabolism
  • Protein Conformation
  • Thylakoids / chemistry
  • Thylakoids / ultrastructure

Substances

  • Bacterial Proteins
  • Photosynthetic Reaction Center Complex Proteins
  • Phycobiliproteins
  • Chlorophyll
  • chlorophyll d