Supramolecular organization of phycobiliproteins in the chlorophyll d-containing cyanobacterium Acaryochloris marina.
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.
Chen
Min
M
School of Biological Sciences, University of Sydney, New South Wales 2006, Australia. minchen@bio.usyd.edu.au
Floetenmeyer
Matthias
M
Bibby
Thomas S
TS
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002734:Chlorophyll / Q000737:chemistry* / Q000378:metabolism; D000458:Cyanobacteria / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D008958:Models, Molecular; D010788:Photosynthesis / Q000502:physiology; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000378:metabolism; D052979:Phycobiliproteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D020524:Thylakoids / Q000737:chemistry / Q000648:ultrastructure
D001426:Bacterial Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D052979:Phycobiliproteins; D002734:Chlorophyll; C107509:chlorophyll d