Isolation, characterization and electron microscopy analysis of a hemidiscoidal phycobilisome type from the cyanobacterium Anabaena sp PCC 7120. Ducret, A, Sidler, W, Wehrli, E, Frank, G, & Zuber, H European Journal of Biochemistry, 236(3):1010–1024, 1996. ![Isolation, characterization and electron microscopy analysis of a hemidiscoidal phycobilisome type from the cyanobacterium Anabaena sp PCC 7120 [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex In this work we present the characterization of a hemidiscoidal phycobilisome type of the heterocyst-forming cyanobacterium Anabaena sp. PCC 7120. The phycobilisome of this organism contains allophycocyanin, phycocyanin and phycoerythrocyanin, similar to the closely related thermophilic cyanobacterium Mastigocladus laminosus. Intact phycobilisomes exhibit an absorption maximum at 619 nm and two fluorescence maxima at 664 nm and 680 nm, corroborating the presence of a complete energy pathway along the antenna. Upon dissociation, the phycobiliproteins were released from the phycobilisome. One phycoerythrocyanin, one phycocyanin and three allophycocyanin complexes were isolated by ion-exchange chromatography and characterized by absorption and fluorescence spectroscopy and by SDS/PAGE. The polypeptides contained in the phycobilisome of Anabaena sp. PCC 7120 were subjected to SDS/PAGE, blotted onto poly(vinylidendifluoride) membranes and identified by amino-terminal sequence analysis. The amino-terminal sequences of the polypeptides belonging to the phycoerythrocyanin and phycocyanin families were identical with the derived sequences of their corresponding genes. Partial amino-terminal sequences of the polypeptides belonging to the allophycocyanin family are presented here. Our results show that the phycobiliproteins and linker polypeptides from Anabaena sp. PCC 7120 are similar to the phycobilisome components characterized in other cyanobacteria. The phycobilisome of Anabaena sp. PCC 7120 was extensively analyzed by electron microscopy. It differs from the common hemidiscoidal tricylindrical, six-rod phycobilisome type by a core domain consisting of five core cylinders surrounded by up to eight rods radiating in a hemidiscoidal manner. One rod is Linked to each basal core cylinder, whereas the remaining core cylinders bind two rods each, On the basis of the data presented in this work, a revised model for the hemidiscoidal pentacylindrical phycobilisome of Anabaena sp. PCC 7120, M. laminosus and Anabaena variabilis is proposed. This model accounts more accurately for the 'grape' pattern typically exhibited by these phycobilisomes in electron micrographs.
@article{ducret_isolation_1996,
title = {Isolation, characterization and electron microscopy analysis of a hemidiscoidal phycobilisome type from the cyanobacterium {Anabaena} sp {PCC} 7120},
volume = {236},
issn = {0014-2956},
url = {http://www.ncbi.nlm.nih.gov/pubmed/8665889},
doi = {10.1111/j.1432-1033.1996.01010.x},
abstract = {In this work we present the characterization of a hemidiscoidal phycobilisome type of the heterocyst-forming cyanobacterium Anabaena sp. PCC 7120. The phycobilisome of this organism contains allophycocyanin, phycocyanin and phycoerythrocyanin, similar to the closely related thermophilic cyanobacterium Mastigocladus laminosus. Intact phycobilisomes exhibit an absorption maximum at 619 nm and two fluorescence maxima at 664 nm and 680 nm, corroborating the presence of a complete energy pathway along the antenna. Upon dissociation, the phycobiliproteins were released from the phycobilisome. One phycoerythrocyanin, one phycocyanin and three allophycocyanin complexes were isolated by ion-exchange chromatography and characterized by absorption and fluorescence spectroscopy and by SDS/PAGE. The polypeptides contained in the phycobilisome of Anabaena sp. PCC 7120 were subjected to SDS/PAGE, blotted onto poly(vinylidendifluoride) membranes and identified by amino-terminal sequence analysis. The amino-terminal sequences of the polypeptides belonging to the phycoerythrocyanin and phycocyanin families were identical with the derived sequences of their corresponding genes. Partial amino-terminal sequences of the polypeptides belonging to the allophycocyanin family are presented here. Our results show that the phycobiliproteins and linker polypeptides from Anabaena sp. PCC 7120 are similar to the phycobilisome components characterized in other cyanobacteria. The phycobilisome of Anabaena sp. PCC 7120 was extensively analyzed by electron microscopy. It differs from the common hemidiscoidal tricylindrical, six-rod phycobilisome type by a core domain consisting of five core cylinders surrounded by up to eight rods radiating in a hemidiscoidal manner. One rod is Linked to each basal core cylinder, whereas the remaining core cylinders bind two rods each, On the basis of the data presented in this work, a revised model for the hemidiscoidal pentacylindrical phycobilisome of Anabaena sp. PCC 7120, M. laminosus and Anabaena variabilis is proposed. This model accounts more accurately for the 'grape' pattern typically exhibited by these phycobilisomes in electron micrographs.},
language = {English},
number = {3},
journal = {European Journal of Biochemistry},
author = {Ducret, A and Sidler, W and Wehrli, E and Frank, G and Zuber, H},
year = {1996},
keywords = {Amino Acid, Amino Acid Sequence, Anabaena, Bacterial Proteins, Cyanobacteria, Electrophoresis, Fluorescence, Light-Harvesting Protein Complexes, Models, Molecular Sequence Data, Molecular Weight, Peptide Fragments, Phycobilins, Phycobilisomes, Phycocyanin, Plant Proteins, Polyacrylamide Gel, Sequence Homology, Spectrometry, Spectrophotometry, Structural, Ultrafiltration, allophycocyanin-b, amino-acid-sequence, c-phycocyanin, core substructure, crystal-structure analysis, cyanobacterium, electron microscopy, light-harvesting antenna, linker-polypeptide complexes, mastigocladus-laminosus phycobilisomes, molecular characterization, photosynthesis, phycobiliprotein, phycobilisome, terminal energy acceptor},
pages = {1010--1024},
}
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Intact phycobilisomes exhibit an absorption maximum at 619 nm and two fluorescence maxima at 664 nm and 680 nm, corroborating the presence of a complete energy pathway along the antenna. Upon dissociation, the phycobiliproteins were released from the phycobilisome. One phycoerythrocyanin, one phycocyanin and three allophycocyanin complexes were isolated by ion-exchange chromatography and characterized by absorption and fluorescence spectroscopy and by SDS/PAGE. The polypeptides contained in the phycobilisome of Anabaena sp. PCC 7120 were subjected to SDS/PAGE, blotted onto poly(vinylidendifluoride) membranes and identified by amino-terminal sequence analysis. The amino-terminal sequences of the polypeptides belonging to the phycoerythrocyanin and phycocyanin families were identical with the derived sequences of their corresponding genes. Partial amino-terminal sequences of the polypeptides belonging to the allophycocyanin family are presented here. Our results show that the phycobiliproteins and linker polypeptides from Anabaena sp. PCC 7120 are similar to the phycobilisome components characterized in other cyanobacteria. The phycobilisome of Anabaena sp. PCC 7120 was extensively analyzed by electron microscopy. It differs from the common hemidiscoidal tricylindrical, six-rod phycobilisome type by a core domain consisting of five core cylinders surrounded by up to eight rods radiating in a hemidiscoidal manner. One rod is Linked to each basal core cylinder, whereas the remaining core cylinders bind two rods each, On the basis of the data presented in this work, a revised model for the hemidiscoidal pentacylindrical phycobilisome of Anabaena sp. PCC 7120, M. laminosus and Anabaena variabilis is proposed. 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