Supramolecular organization of phycobiliproteins in the chlorophyll d-containing cyanobacterium Acaryochloris marina
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.
Abbreviations: CBPs, accessory chlorophyll-binding-proteins, Chl, chlorophyll, PBP, phycobiliprotein, PS, photosystem, PBS, phycobilisome, PC, phycocyanin, APC, allophycocyanin, TEM, transmission electron microscopy, CEMOVIS, cryo-electron microscopy of vitreous sections, TM, thylakoid membranes
Keywords: Phycobiliprotein, Cryo-electron microscopy, Membrane organization, Acaryochloris marina
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PII: S0014-5793(09)00537-7
doi:10.1016/j.febslet.2009.07.012
© 2009 Federation of European Biochemical Societies
