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Updated: May 5, 2026

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
Published on: November 10, 2021
Accessory polypeptides in phycobilisomes of red algae and cyanobacteria
1Fachbereich Biologie, Zellbiologie und Entwicklungsphysiologie der Pflanzen, Universität Marburg, Karl-von-Frisch-Strasse, D-3550, Marburg, Federal Republic of Germany.
Abstract:
Phycobilisomes of red algae and cyanobacteria contain small amounts of nonpigmented polypeptides in addition to the major constituent biliprotein pigments. The localization of these polypeptides is analyzed by gel electrophoresis of phycobilisome fragments obtained by selective dissociation and subsequent separation. Five groups of biliprotein aggregates are determined, belonging to the 6, 11, 16, 18 and 23 S categories. Accessory nonpigmented high molecular weight proteins (80,000 MW) are exclusively bound to phycobilisome core fractions and thylakoids, thus apparently serving as links between the phycobilisomes and the photosynthetic units of the thylakoids. In contrast, smaller nonpigmented accessory polypeptides of 20,000 to 60,000 MW are preferably found in the peripheral biliprotein stacks. They may either form a compatible link between the phycobilisome core and periphery or bind and co-polymerize with hexameric biliproteins in the peripheral stacks to enhance or effect binding of the aggregates. Furthermore, they may determine the arrangement and composition of the phycobilisomes during development and chromatic adaptation.
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