![]() ![]() Light serves as an essential energy source for life on earth. We propose that the CpcL-PBS and the rod-core PBS fulfill distinct functions in light harvesting. ![]() Our results suggest that CpcL and CpcG4 compete for the same phycobiliprotein pool, and therefore the CpcL/CpcG4 ratio determines the levels of PBS-PSI supercomplexes. In both mutant strains, more and larger PBS-PSI supercomplexes accumulated compared to the wild type. Here, we analyzed two mutant strains which either lack the major rod-core linker CpcG4 or overexpress the rod-membrane linker CpcL. How cells control the accumulation of the two different types of PBS is unknown. The CpcL-PBS and the rod part of the rod-core PBS are identical except for the linker proteins CpcL and CpcG. PCC 7120, the CpcL-PBS forms a complex with the tetrameric PSI (PBS-PSI supercomplex). In the filamentous heterocyst-forming cyanobacterium Anabaena ( Nostoc) sp. ![]() This rod-type PBS is connected to the thylakoid membrane by the linker protein CpcL and is a PSI-specific antenna. Cyanobacteria assemble another type of PBS, the CpcL-PBS, which consists of only one rod. The rod-core PBS transfers the light energy mainly to photosystem (PS) II and to a lesser extent to PSI. In the standard PBS, the rod-core PBS, the rods are connected to the core by the rod-core linker protein CpcG. The phycobilisome (PBS) is an antenna protein complex in cyanobacteria, Glaucocystophytes, and red algae. ![]()
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