Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 68:1375-1379 (1981)
© 1981 American Society of Plant Biologists

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Articles

Phycobilisome Structure of Porphyridium cruentum1

POLYPEPTIDE COMPOSITION

Thomas Redlinger and Elisabeth Gantt

Radiation Biology Laboratory, Smithsonian Institution, 12441 Parklawn Drive, Rockville, Maryland 20852

Purified phycobilisomes of Porphyridium cruentum were solubilized in sodium dodecyl sulfate and resolved by sodium dodecyl sulfate-acrylamide gel electrophoresis into nine colored and nine colorless polypeptides. The colored polypeptides accounted for about 84% of the total stainable protein, and the colorless polypeptides accounted for the remaining 16%. Five of the colored polypeptides ranging in molecular weight from 13,300 to 19,500 were identified as the {alpha} and beta subunits of allophycocyanin, R-phycocyanin, and phycoerythrin. Three others (29,000-30,500) were orange and are probably related to the {gamma} subunit of phycoerythrin. Another colored polypeptide had a molecular weight of 95,000 and the characteristics of long wavelength-emitting allophycocyanin. Sequential dissociation of phycobilisomes, and analysis of the polypeptides in each fraction, revealed the association of a 32,500 molecular weight colorless polypeptide with a phycoerythrin fraction. The remaining eight colorless polypeptides were in the core fraction of the phycobilisome, which also was enriched in allophycocyanin. In addition, the core fraction was enriched in a colored 95,000 dalton polypeptide. Inasmuch as a polypeptide with the same molecular weight is found in thylakoid membranes (free of phycobilisomes), it is suggested that this polypeptide is involved in anchoring phycobilisomes to thylakoid membranes.

1 Supported in part by a Smithsonian Postdoctoral Fellowship to T. R. and by Contract AS 05-76-ER 04310 from the Department of Energy.




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