Extensive remodeling of the photosynthetic apparatus alters energy transfer among photosynthetic complexes when cyanobacteria acclimate to far-red light

Ho, Ming-Chih; Niedzwiedzki, Dariusz M.; MacGregor-Chatwin, Craig; Gerstenecker, Gary; Hunter, C. Neil; Blankenship, Robert E.; Bryant, Donald A.

doi:10.1016/j.bbabio.2019.148064

Cited by 54 publications

(71 citation statements)

References 63 publications

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“…Because PsaJ is located on the periphery of the PSI trimer, it could be that in WL-PSI, these pigments provide bridges to transfer energy to/from another protein in a supercomplex array (21). Arrays of PSI trimers, dimers, and monomers associated with PSII dimers have been observed in thylakoid membranes by atomic force microscopy imaging (22). PsaJ2 does not coordinate pigments, implying that these interactions might be altered in FRL-PSI.…”

Section: Structural Observations and Differences In Pigment Binding Smentioning

confidence: 99%

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The structure of Photosystem I acclimated to far-red light illuminates an ecologically important acclimation process in photosynthesis

et al. 2020

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Phototrophic organisms are superbly adapted to different light environments but often must acclimate to challenging competition for visible light wavelengths in their niches. Some cyanobacteria overcome this challenge by expressing paralogous photosynthetic proteins and by synthesizing and incorporating ~8% chlorophyll f into their Photosystem I (PSI) complexes, enabling them to grow under far-red light (FRL). We solved the structure of FRL-acclimated PSI from the cyanobacterium Fischerella thermalis PCC 7521 by single-particle, cryo–electron microscopy to understand its structural and functional differences. Four binding sites occupied by chlorophyll f are proposed. Subtle structural changes enable FRL-adapted PSI to extend light utilization for oxygenic photosynthesis to nearly 800 nm. This structure provides a platform for understanding FRL-driven photosynthesis and illustrates the robustness of adaptive and acclimation mechanisms in nature.

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Section: Structural Observations and Differences In Pigment Binding Smentioning

confidence: 99%

“…S7B). Recall that Chl F1 is not present in the FRL-PSI structure and the amino acid that provides its axial coordination, PsaJ2 Thr 22 is not conserved (Fig. 3B and fig.…”

Section: Chl B37mentioning

confidence: 99%

The structure of Photosystem I acclimated to far-red light illuminates an ecologically important acclimation process in photosynthesis

et al. 2020

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“…The multitude of cryo-EM structures emerging in the literature recently has profoundly contributed to our understanding of the diversity of phototrophy on the molecular scale and this trend appears likely to continue and even expand. There are multiple Chl types in other reaction centers, photosystems, and antenna complexes, such as those found in FRL-PSII 29 , 75 , the photosystems of Acaryochloris marina 58 , 76 , Candidatus Chloracidobacterium (Cab.) thermophilum 77 , and possibly others not yet discovered.…”

Section: Outlook For Cryo-em In Photosynthesis Researchmentioning

confidence: 99%

Opportunities and challenges for assigning cofactors in cryo-EM density maps of chlorophyll-containing proteins

et al. 2020

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The accurate assignment of cofactors in cryo-electron microscopy maps is crucial in determining protein function. This is particularly true for chlorophylls (Chls), for which small structural differences lead to important functional differences. Recent cryo-electron microscopy structures of Chl-containing protein complexes exemplify the difficulties in distinguishing Chl b and Chl f from Chl a . We use these structures as examples to discuss general issues arising from local resolution differences, properties of electrostatic potential maps, and the chemical environment which must be considered to make accurate assignments. We offer suggestions for how to improve the reliability of such assignments.

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“…Cryogenic detection helped to monitor energy transfer in FRL-adapted Synechococcus sp. PCC 7335 [55]. Purified PSI or PSII preparations obtained from FRL-adapted cells showed one and the same well-expressed peak at 738-740 nm indicating similar effectiveness of energy coupling notwithstanding a distinction in PS structure.…”

Section: Fluorescence Methods Employed In the Research Of Far-red Ligmentioning

confidence: 81%

“…Time-resolved fluorescence spectroscopy also helped to analyze energy transfer in RL-or FRL-grown cells of Synechococcus sp. PCC 7335 [55], as well as in A. marina mini PBS [63].…”

Section: Time-resolved Fluorescence Spectroscopymentioning

confidence: 98%

Far-Red Light Absorbing Photosynthetic Pigments in Cyanobacteria: Steady-State Fluorescence Detection, Time-Resolved Fluorescence Spectroscopy, and Confocal Laser Scanning Microscopy

Averina¹,

Senatskaya²,

Пиневич³

2020

Fluorescence Methods for Investigation of Living Cells and Microorganisms

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The use of far-red light (FRL) is observed in some cyanobacteria, as well as in some marine and freshwater algae. While algae mobilize FRL absorbing antenna, which contains common chlorophyll a (Chl a), cyanobacteria produce red-shifted Chl d and/or Chl f. These pigments are synthesized either irrespective of ambient light or synthesized during FRL photoacclimation (FaRLiP), or adaptive remodeling of photosynthetic apparatus induced by relative enrichment with FRL quanta. The presence of red-shifted chlorophylls as well as their functions and topography are registered with various methods based on fluorescence measurement, such as: (1) steady-state fluorescence detection in live cells, cell fractions, and photosynthetic apparatus constituents; (2) time-resolved fluorescence spectroscopy, which traces energy transfer between individual pigments; (3) confocal laser scanning microscopy (CLSM), which helps to localize photosynthetic pigments in situ. This chapter describes photosynthetic apparatus in cyanobacteria and their photoacclimation phenomena. Over past decades, FRL photoacclimation has been studied in a small number of cyanobacteria. Novel Chl f-producing strains Chlorogloeopsis sp. CALU 759 and Synechocystis sp. CALU 1173 would represent promising model objects. Importantly, although they belong to alternative morphotypes and distant phylogenetic lineages, fluorescence pattern of their FRL-grown cells similarly falls within general FaRLiP response.

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Extensive remodeling of the photosynthetic apparatus alters energy transfer among photosynthetic complexes when cyanobacteria acclimate to far-red light

Cited by 54 publications

References 63 publications

The structure of Photosystem I acclimated to far-red light illuminates an ecologically important acclimation process in photosynthesis

The structure of Photosystem I acclimated to far-red light illuminates an ecologically important acclimation process in photosynthesis

Opportunities and challenges for assigning cofactors in cryo-EM density maps of chlorophyll-containing proteins

Far-Red Light Absorbing Photosynthetic Pigments in Cyanobacteria: Steady-State Fluorescence Detection, Time-Resolved Fluorescence Spectroscopy, and Confocal Laser Scanning Microscopy

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