Distinct roles of CpcG1 and CpcG2 in phycobilisome assembly in the cyanobacterium Synechocystis sp. PCC 6803.
Structural role of the second copy of the rod-core linker CpcG, which was found by genome analysis, was studied in Synechocystis sp. PCC 6803 by gene disruption and fractionation of phycobilisome (sub)complexes. Disruption of cpcG2 (sll1471) resulted in a marked decrease in phycocyanin content both in the background of wild-type and cpcG1 (slr2051)-disruptant. The unique phycocyanin rod-CpcG2 complex without the major allophycocyanin components was isolated from the cpcG1-disruptant. By fluorescence analysis, it was proposed that CpcG2 protein connects the rods with a minor allophycocyanin component, to support energy transfer to Photosystem I.
Kondo
Kumiko
K
Department of Biological Science, Graduate School of Sciences, University of Tokyo, Komaba, Meguro, Tokyo 153-8902, Japan.
Geng
Xiao Xing
XX
Katayama
Mitsunori
M
Ikeuchi
Masahiko
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D004735:Energy Transfer; D017353:Gene Deletion; D045524:Phycobilisomes / Q000737:chemistry / Q000378:metabolism*; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D046939:Synechocystis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D045524:Phycobilisomes