Role of the PB-loop in ApcE and phycobilisome core function in cyanobacterium Synechocystis sp. PCC 6803

Zlenko, Dmitry V.; Elanskaya, I.V.; Лукашев, Е. П.; Bolychevtseva, Yu. V.; Suzina, N. E.; Pojidaeva, E. S.; Kononova, Irena A.; Loktyushkin, A. V.; Stadnichuk, Igor N.

doi:10.1016/j.bbabio.2018.10.004

Cited by 28 publications

(18 citation statements)

References 78 publications

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“…41,43 In the ApcE-C190S and the PB-loop ApcE Synechocystis mutants, the energy transfer from PBS to the photosystems is significantly affected. 43,44 However, state transitions in the former are not impaired, 91 while they appear to be decreased in the latter. 44 It has been proposed that the impairment of state transitions in the ΔApcD Synechocystis mutant is due to a permanent binding of PBS to PSII, which increases the PSII antenna even in darkness and PSII illumination (when the PQ pool is reduced).…”

Section: Pbs Mutants Impaired In State Transitionsmentioning

confidence: 90%

“…43,44 However, state transitions in the former are not impaired, 91 while they appear to be decreased in the latter. 44 It has been proposed that the impairment of state transitions in the ΔApcD Synechocystis mutant is due to a permanent binding of PBS to PSII, which increases the PSII antenna even in darkness and PSII illumination (when the PQ pool is reduced). 41 This hypothesis can explain the relatively high fluorescence observed in the dark-adapted ΔApcD Synechocystis cells.…”

Section: Pbs Mutants Impaired In State Transitionsmentioning

confidence: 90%

“…Mutations in ApcD, ApcF 40,41,51,85 and a particular domain of ApcE 44 affect state transitions in several cyanobacterial strains (Table 3). 40 suggested that in the ΔApcD Synechococcus PCC 7002 mutant, the inhibition of state transitions was due to a permanent decrease in energy transfer from PBS to PSI.…”

Section: Pbs Mutants Impaired In State Transitionsmentioning

confidence: 99%

“…Mutations in the PBS terminal emitters affect the energy transfer to one or both photosystems in different cyanobacterial strains (see discussion in following sections). [40][41][42][43][44] The entire scientific community agrees that in cyanobacteria, like in plants and green algae, state transitions are triggered by redox changes in the PQ pool. 45,46 However, no agreement can be found in literature about the molecular mechanism, the sensor of the PQ redox state, or the signaling pathways involved.…”

Section: Introductionmentioning

confidence: 99%

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Revisiting cyanobacterial state transitions

Calzadilla

Kirilovsky

2020

Photochem Photobiol Sci

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Section: Pbs Mutants Impaired In State Transitionsmentioning

confidence: 90%

Section: Pbs Mutants Impaired In State Transitionsmentioning

confidence: 90%

Section: Pbs Mutants Impaired In State Transitionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Revisiting cyanobacterial state transitions

Calzadilla

Kirilovsky

2020

Photochem Photobiol Sci

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“…PBS cores were isolated from the disrupted CK‐mutant cells by sucrose density gradient ultracentrifugation as it was described earlier . PSII complexes were obtained from the thylakoid membranes of PAL mutant solubilized by n ‐dodecyl‐β‐ d maltoside using one‐step chromatography (Toyopearl DEAE 650 S resin; Tosoh, Tokyo, Japan) according to the protocol described by Kern et al .…”

Section: Methodsmentioning

confidence: 99%

Rates and pathways of energy migration from the phycobilisome to the photosystem II and to the orange carotenoid protein in cyanobacteria

2019

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Edited by Ulf-Ingo Fl€ uggeThe phycobilisome (PBS) is the cyanobacterial antenna complex which transfers absorbed light energy to the photosystem II (PSII), while the excess energy is nonphotochemically quenched by interaction of the PBS with the orange carotenoid protein (OCP). Here, the molecular model of the PBS-PSII-OCP supercomplex was utilized to assess the resonance energy transfer from PBS to PSII and, using the excitonic theory, the transfer from PBS to OCP. Our estimates show that the effective energy migration from PBS to PSII is realized due to the existence of several transfer pathways from phycobilin chromophores of the PBS to the neighboring antennal chlorophyll molecules of the PSII. At the same time, the single binding site of photoactivated OCP and the PBS is sufficient to realize the quenching.

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Absence of the Third Linker Domain of ApcE Subunit in Phycobilisome from Synechocystis 6803 Reduces Rods‐To‐Core Excitation Energy Transfer

Niedzwiedzki,

Tomar,

Akram

et al. 2024

ChemPhysChem

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Phycobilisome (PBS) is a pigment‐protein complex utilized by red algae and cyanobacteria in photosynthesis for light harvesting. A cyanobacterium Synechocystis sp. PCC 6803 contains PBS with a tricylindrical core built of allophycocyanin (APC) disks where six phycocyanin (PC) rods are attached. The top core cylinder is seemingly involved in attaching four PC rods and binding orange carotenoid protein (OCP) to quench excess of excitation energy. In this study, we have deleted the third linker domain (LD3) of ApcE subunit of PBS which assembles four APC discs into the top core cylinder. The mutation resulted in PBS with bicylindrical core, structurally comparable to the naturally existing PBS from Synechococcus 7942. Lack of LD3 and the top APC cylinder reduces the excitation energy transfer between PC and APC in the mutant. Moreover, these PBSs are more prone to light induced‐photodamage and do not bind to the photoactivated orange carotenoid protein (OCP), a known PBS excitation quencher. These findings highlight the complex and elegant interplay between PBS architecture and functional efficiency, suggesting that in PBSs with naturally tri‐cylindrical cores, the top cylinder has essential roles in recruiting the rods and proper binding of OCP and recruitment of the four PC rods.

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Role of the PB-loop in ApcE and phycobilisome core function in cyanobacterium Synechocystis sp. PCC 6803

Cited by 28 publications

References 78 publications

Revisiting cyanobacterial state transitions

Revisiting cyanobacterial state transitions

Rates and pathways of energy migration from the phycobilisome to the photosystem II and to the orange carotenoid protein in cyanobacteria

Absence of the Third Linker Domain of ApcE Subunit in Phycobilisome from Synechocystis 6803 Reduces Rods‐To‐Core Excitation Energy Transfer

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