Gloeobacter violaceus is an ancient cyanobacterium as it branches out from the basal position in the phylogenic tree of cyanobacteria. It lacks thylakoid membranes and its unique bundle-shaped type of phycobilisomes (PBS) for light harvesting in photosynthesis are located on the interior side of cytoplasmic membranes. The PBS from G. violaceus have two large linker proteins that are not present in any other PBS, Glr2806, and Glr1262, which are encoded by the genes glr2806 and glr1262, respectively. The location and functions of the linkers Glr2806 and Glr1262 are currently unclear. Here, we report the studies of mutagenetic analysis of glr2806 and the genes of cpeBA, encoding the β and α subunits of phycoerythrin (PE), respectively. In the mutant lacking glr2806, the length of the PBS rods remains unchanged, but the bundles are less tightly packed as examined by electron microscopy with negative staining. It is also shown that two hexamers are missing in the peripheral area of the PBS core, strongly suggesting that the linker Glr2806 is located in the core area instead of the rods. In the mutant lacking the cpeBA genes, PE is no longer present and the PBS rods have only three layers of phycocyanin hexamers. The construction of deletional mutants in G. violaceus, achieved for the first time, provides critical information for our understanding of its unique PBS and should be useful in studies of other aspects of this interesting organism as well.
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