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Electron microscopic analysis of native bili protein aggregates and their spatial assembly


, : Electron microscopic analysis of native bili protein aggregates and their spatial assembly. Berichte der Deutschen Botanischen Gesellschaft 92(2-3): 393-402

The biliproteins of the cryptomonad algae Cryptomonas maculata (phycoerythrin-545), Chroomonas sp. (phycocyanin-645) and Hemiselmis rufescens (phycoerythrin-555) can be isolated in the assembly form of dimers (.alpha.beta.)2. In ultrathin sections of structurally well-preserved cells they are present either dispersed within the lumina of the thylakoids or, locally, in fine rows of columns oriented at right angles to the inner surface of the thylakoid membranes. The biliproteins B-phycoerythrin, C-phycocyanin and allophycocyanin of the unicellular red alga Rhodella violacea are aggregated in vivo in phycobilisomes attached to the outer surface of the thylakoid membranes. At higher magnification isolated native C-phycocyanin and allophycocyanin consist of 6 globular protein subunits arranged in ring-like structures with a central hole. These aggregates can be regarded as trimers (.alpha.beta.)3. Native B-phycoerythrin consists also of a 6 membered periphery but containing a central subunit, which keeps 2 rings of globular protein subunits face to face. Tripartite units, a well-defined structural element of the phycobilisome periphery in R. violacea, contain phycoerythrin and phycocyanin in a molar ratio of 2:1. Each of the 3 discs of the tripartite unit has a similar morphology in profile and consists of 2 rings of globular protein subunits. This confirms the observations with native B-phycoerythrin isolates and supports the view of a face to face aggregation of 2 trimeric C-phycocyanin rings in vivo to make up 1 part of the tripartite unit. An improved model of the phycobilisome of R. violacea is presented.

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