Abstract
ABSTRACTThe acclimation of cyanobacteria to iron deficiency is crucial for their survival in natural environments. In response to iron deficiency, many cyanobacterial species induce the production of a pigment-protein complex called IsiA. IsiA proteins associate with photosystem I (PSI) and can function as light-harvesting antennas or dissipate excess energy. They may also serve as Chl storage during iron limitation. In this study we examined the functional role of IsiA in cells ofSynechocystissp. PCC 6803 grown under iron limitation conditions by measuring the cellular IsiA content and its capability to transfer energy to PSI. We specifically test the effect of the oligomeric state of PSI by comparing wild-type (WT)Synechocystissp. PCC 6803 to mutants lacking specific subunits of PSI, namely PsaL/PsaI (ΔpsaLmutant) and PsaF/PsaJ (ΔFIJL). Time-resolved fluorescence spectroscopy revealed that IsiA formed functional PSI3-IsiA18supercomplexes, wherein IsiA effectively transfers energy to PSI on a timescale of 10 ps at room temperature – measured in isolated complexes and in vivo – confirming the primary role of IsiA as an accessory light-harvesting antenna to PSI. However, a significant fraction (40%) remained unconnected to PSI, supporting the notion of a dual functional role of IsiA. Cells with monomeric PSI under iron deficiency contained only 3–4 IsiA complexes bound to PSI. Together the results show that IsiA is capable of transferring energy to trimeric and monomeric PSI but to varying degrees and that the acclimatory production of IsiA under iron stress is controlled by its ability to perform its light-harvesting function.
Publisher
Cold Spring Harbor Laboratory