The linker protein ApcI regulates light harvesting under red light in Synechocystis sp. PCC 6803

. 2025 Jul 01 ; 37 (7) : .

Jazyk angličtina Země Anglie, Velká Británie Médium print

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid40479507

Grantová podpora
DE-SC0020606 U.S. Department of Energy
DE-SC0010847 laboratory of W.F.B.
Office of Basic Energy Sciences
LUAUS24149 Ministry of Education, Youth and Sports of CR
LM2018123 CzeCOS program
CZ.02.1.01/0.0/0.0/16 026/0008413 OP RDE

Phycobilisomes (PBSs) are versatile cyanobacterial antenna complexes that harvest light energy to drive photosynthesis. They can adapt to various light conditions; for example, dismantling under high light to prevent photo-oxidation and arranging in rows under low light to increase light harvesting efficiency. Light quality also influences PBS structure and function, as observed under far-red light exposure. Here, we describe a PBS linker protein, ApcI (previously hypothetical protein Sll1911), expressed specifically under red light (620 nm) or upon chemically induced reduction of the plastoquinone pool. We characterized ApcI in Synechocystis sp. PCC 6803 using mutant analyses, PBS binding experiments, and protein interaction studies. Deletion of apcI conferred high light tolerance on Synechocystis sp. PCC 6803 compared to the wild-type strain, leading to reduced energy transfer from PBSs to the photosystems under high light. Binding experiments revealed that ApcI replaces the linker protein ApcG at the membrane-facing side of the PBS core via a paralogous C-terminal motif. Additionally, the N-terminal region of ApcI interacts with photosystem II. Our findings highlight the importance of PBS remodeling for adaptation to different light conditions. The characterization of ApcI provides insight into the mechanisms by which cyanobacteria optimize light harvesting in response to varying light conditions.

Citace poskytuje Crossref.org

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