Altered excitation energy transfer between phycobilisome and photosystems in the absence of ApcG, a small linker peptide, in Synechocystis sp. PCC 6803, a cyanobacterium
Journal Article
·
· Biochimica et Biophysica Acta - Bioenergetics
- Saint Louis University, MO (United States); Saint Louis University
- Washington University in St. Louis, MO (United States); Saint Louis University, MO (United States)
- Saint Louis University, MO (United States)
Phycobilisome (PBS) is a large pigment-protein complex in cyanobacteria and red algae responsible for capturing sunlight and transferring its energy to photosystems (PS). Spectroscopic and structural properties of various PBSs have been widely studied, however, the nature of so-called complex-complex interactions between PBS and PSs remains much less explored. In this work, we have investigated the function of a newly identified PBS linker protein, ApcG, some domain of which, together with a loop region (PB-loop in ApcE), is possibly located near the PBS-PS interface. Using Synechocystis sp. PCC 6803, we generated an ApcG deletion mutant and probed its deletion effect on the energetic coupling between PBS and photosystems. Steady-state and time-resolved spectroscopic characterization of the purified ΔApcG-PBS demonstrated that ApcG removal weakly affects the photophysical properties of PBS that the spectroscopic properties of terminal energy emitters are comparable to those of PBS from wild-type. However, analysis of fluorescence decay imaging datasets reveals that ApcG deletion induces disruptions within the allophycocyanin (APC) core, resulting in the emergence (splitting) of two spectrally diverse subgroups with some short-lived APC. Profound spectroscopic changes of the whole ΔApcG mutant cell, however, emerge during state transition, a dynamic process of light scheme adaptation. The mutant cells in State I show a substantial increase in PBS-related fluorescence. On the other hand, global analysis of time-resolved fluorescence demonstrates that in general ApcG deletion does not alter or inhibit state transitions if it is interpreted only in terms of the changes of the PSII and PSI fluorescence emission intensity. Furthermore, the results revealed yet–to–be discovered mechanism of ApcG-docking induced excitation energy transfer regulation within PBS or to Photosystems.
- Research Organization:
- Saint Louis University, MO (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- FG02-07ER15902
- OSTI ID:
- 2368560
- Journal Information:
- Biochimica et Biophysica Acta - Bioenergetics, Journal Name: Biochimica et Biophysica Acta - Bioenergetics Journal Issue: 3 Vol. 1865; ISSN 0005-2728
- Publisher:
- ElsevierCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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