Effect of APCD and APCF subunits depletion on phycobilisome fluorescence of the cyanobacterium Synechocystis PCC 6803

Kuzminov, Fedor I.; Bolychevtseva, Yu. V.; Elanskaya, I.V.; Karapetyan, N. V.

doi:10.1016/j.jphotobiol.2014.03.012

Cited by 15 publications

(18 citation statements)

References 38 publications

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“…According to spectroscopic data obtained by Kuzminov et al [42], β 18 should transfer energy to the LC M , a fact that could be accomplished only if they are in the same trimer but neighboring heterodimers. Finally, they propose that β 18 is a mediator in the energy transfer towards the final emitter, with the chromophore present in the L CM (PB_domain).…”

Section: Resultsmentioning

confidence: 99%

Structural models of the different trimers present in the core of phycobilisomes from Gracilaria chilensis based on crystal structures and sequences

et al. 2017

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Phycobilisomes (PBS) are accessory light harvesting protein complexes that directionally transfer energy towards photosystems. Phycobilisomes are organized in a central core and rods radiating from it. Components of phycobilisomes in Gracilaria chilensis (Gch) are Phycobiliproteins (PBPs), Phycoerythrin (PE), and Phycocyanin (PC) in the rods, while Allophycocyanin (APC) is found in the core, and linker proteins (L). The function of such complexes depends on the structure of each component and their interaction. The core of PBS from cyanobacteria is mainly composed by cylinders of trimers of α and β subunits forming heterodimers of Allophycocyanin, and other components of the core including subunits αII and β18. As for the linkers, Linker core (LC) and Linker core membrane (LCM) are essential for the final emission towards photoreaction centers. Since we have previously focused our studies on the rods of the PBS, in the present article we investigated the components of the core in the phycobilisome from the eukaryotic algae, Gracilaria chilensis and their organization into trimers. Transmission electron microscopy provided the information for a three cylinders core, while the three dimensional structure of Allophycocyanin purified from Gch was determined by X-ray diffraction method and the biological unit was determined as a trimer by size exclusion chromatography. The protein sequences of all the components of the core were obtained by sequencing the corresponding genes and their expression confirmed by transcriptomic analysis. These subunits have seldom been reported in red algae, but not in Gracilaria chilensis. The subunits not present in the crystallographic structure were modeled to build the different composition of trimers. This article proposes structural models for the different types of trimers present in the core of phycobilisomes of Gch as a first step towards the final model for energy transfer in this system.

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Section: Resultsmentioning

confidence: 99%

Structural models of the different trimers present in the core of phycobilisomes from Gracilaria chilensis based on crystal structures and sequences

et al. 2017

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“…A second α unit is replaced by the globular domain (PB domain) of the Linker core-membrane (ApcE) [18] , [45] . ApcD, ApcF and PB domain are essential to energy tansfer to the photosystems [46] , [47] , [48] , [49] …”

Section: Structural Characteristics Of Pbpsmentioning

confidence: 99%

Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives

Dagnino‐Leone

Figueroa

Castañeda

et al. 2022

Computational and Structural Biotechnology Journal

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“…PCC 6803 engineered to be deficient of PSI/PSII, PSI/PSII/APCD, and PSI/PSII/ APCF. 23 They found that the transition at 665 nm always involved β 18 . Further, they found that the transition 680 nm involved the coupling of L CM (encoding APC E and the once encoding APC D) with β in an adjacent monomer in an APClike trimer.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Cryospectroscopy Studies of Intact Light-Harvesting Antennas Reveal Empirical Electronic Energy Transitions in Two Cyanobacteria Species

2018

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Understanding of electronic energy transition (EET) mechanisms from the light-harvesting unit to the reaction center in a natural system has been limited by (a) the use of conventional transient time-resolved spectroscopy at room temperature, which result in high signal-to-noise ratio and (b) examining extracts instead of intact light-harvesting units. Here, we report previously unknown differences and new insight in EET of two cyanobacteria species, Acaryochloris marina and Thermosynechoccocus vulcanus, which have been found only after using UV-vis, hole-burning, and fluorescence spectroscopy at ultralow temperature and examining their intact light-harvesting unit, phycobilisomes (PBS). Although the exciton formation is similarly induced by photoexcitation of chromophore assemblies in phycocyanin (PC) and allophycocyanin (APC) in PBSs of both species, the EET mechanisms are totally different, being adiabatic in A. marina and nonadiabatic in T. vulcanus. The PBS of A. marina has only one APC trimer and energy transfer is through coupling of α in APC with β in adjacent PC. In T. vulcanus, the PBS has three components: coupling between APC core and the entire PC rod and couplings of β-β and of L to β in the adjacent APC-like trimer. A total of 80% of the excitation energy is trapped in the coupling β-β and regulates the flow of energy from the high- to low-level terminal electronic transition emitter β-L. All these details cannot be observed at room temperature and in extracted units.

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Effect of APCD and APCF subunits depletion on phycobilisome fluorescence of the cyanobacterium Synechocystis PCC 6803

Cited by 15 publications

References 38 publications

Structural models of the different trimers present in the core of phycobilisomes from Gracilaria chilensis based on crystal structures and sequences

Structural models of the different trimers present in the core of phycobilisomes from Gracilaria chilensis based on crystal structures and sequences

Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives

Cryospectroscopy Studies of Intact Light-Harvesting Antennas Reveal Empirical Electronic Energy Transitions in Two Cyanobacteria Species

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