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PHYCOBILIPROTEIN COMPONENTS AND CHARACTERISTICS OF THE PHYCOBILISOME FROM A THERMOPHILIC CYANOBACTERIUM MYXOSARCINA CONCINNA1
Article first published online: 20 OCT 2011
© 2011 Phycological Society of America
Journal of Phycology
Volume 47, Issue 6, pages 1304–1315, December 2011
How to Cite
Sun, L. and Wang, S. (2011), PHYCOBILIPROTEIN COMPONENTS AND CHARACTERISTICS OF THE PHYCOBILISOME FROM A THERMOPHILIC CYANOBACTERIUM MYXOSARCINA CONCINNA. Journal of Phycology, 47: 1304–1315. doi: 10.1111/j.1529-8817.2011.01067.x
Received 24 January 2010. Accepted 6 May 2011.
- Issue published online: 1 DEC 2011
- Article first published online: 20 OCT 2011
- linker polypeptide;
- Myxosarcina concinna;
A phycocyanin (PC) and three allophycocyanin (AP) components (designated PC, AP1, AP2, and AP3) were prepared from Myxosarcina concinna Printz phycobilisomes by the native gradient PAGE performed in a neutral buffer system combined with the ion exchange column chromatography on DEAE-DE52 cellulose. PC contained one β subunit () and two α ones ( and ), and it carried two rod linkers ( and ) and one rod-core linker (). AP1 and AP3 were characterized as peripheral core APs, whereas AP2 was an inner-core one. AP2 and AP3 were demonstrated to function as the terminal emitters. Each of the three APs contained two β subunits ( and ), two α subunits ( and ) and an inner-core linker (). AP2 and AP3 had another subunit of the allophycocyanin B (AP-B) type () belonging to the β subunit group, and AP1 and AP3 carried their individual specific core linkers ( and ), respectively. No AP component was shown to associate with the core-membrane linker LCM. The functions of the linker polypeptides in the phycobilisome (PBS) construction are discussed.