The diversity and distribution of D1 proteins in cyanobacteria

Sheridan, Kevin J.; Duncan, Elizabeth J.; Eaton‐Rye, Julian J.; Summerfield, Tina C.

doi:10.1007/s11120-020-00762-7

Cited by 28 publications

(40 citation statements)

References 86 publications

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“…The unrooted phylogeny of D1 is shown in figure 2 and is similar to those presented by previous authors ( Sheridan et al 2020 ). Photosystem II adapts to changing environments by swapping D1 subunits to variant forms better tuned to new conditions.…”

Section: Resultssupporting

confidence: 84%

Complete Genome Sequencing of a NovelGloeobacterSpecies from a Waterfall Cave in Mexico

Saw

Cardona

Montejano

2021

Genome Biology and Evolution

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Only two complete genomes of the cyanobacterial genus Gloeobacter from two very different regions of the world currently exist. Here we present the complete genome sequence of a third member of the genus isolated from a waterfall cave in Mexico. Analysis of the average nucleotide identities (ANI) between published Gloeobacter genomes revealed that the complete genome of this new member is only 92.7% similar to Gloeobacter violaceus and therefore we determined it to be a new species. We propose to name this new species Gloeobacter morelensis after the location in Mexico where it was isolated. The complete genome consists of one circular chromosome (4,921,229 bp), one linear plasmid (172,328 bp), and one circular plasmid (8,839 bp). Its genome is the largest of all completely sequenced genomes of Gloeobacter species. Pangenomic comparisons revealed that G. morelensis encodes 759 genes not shared with other Gloeobacter species. Despite being more closely related to G. violaceus, it features an extremely divergent psbA gene encoding an atypical D1 core subunit of Photosystem II previously only found within the genome of G. kilaueensis. In addition, we detected evidence of concerted evolution of psbA genes encoding identical D1 in all three Gloeobacter genomes, a characteristic that seems widespread in cyanobacteria and may therefore be traced back to their last common ancestor.

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Section: Resultssupporting

confidence: 84%

Complete Genome Sequencing of a NovelGloeobacterSpecies from a Waterfall Cave in Mexico

Saw

Cardona

Montejano

2021

Genome Biology and Evolution

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“…To provide insight into the evolution of the FRL-PSII subunits, we generated phylogenetic trees for each of the core subunits: PsbA, PsbD, PsbC, PsbB, and PsbH (Figure 1 and Supplementary Figures S1−S5). The evolution of PsbA has been studied in detail [35][36][37][38] and the tree shown in Figure 1 is generally consistent with those shown before. The tree includes two PsbA paralogs of importance for FaRLiP: (1) the Chl f synthase, also known as ChlF [39][40][41] or Group 1 (G1); and (2) FRL-PsbA, which enables water oxidation under FaRLiP.…”

Section: Phylogenetic Analysissupporting

confidence: 83%

Molecular Evolution of Far-Red Light-Acclimated Photosystem II

et al. 2022

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Cyanobacteria are major contributors to global carbon fixation and primarily use visible light (400−700 nm) to drive oxygenic photosynthesis. When shifted into environments where visible light is attenuated, a small, but highly diverse and widespread number of cyanobacteria can express modified pigments and paralogous versions of photosystem subunits and phycobiliproteins that confer far-red light (FRL) absorbance (700−800 nm), a process termed far-red light photoacclimation, or FaRLiP. During FaRLiP, alternate photosystem II (PSII) subunits enable the complex to bind chlorophylls d and f, which absorb at lower energy than chlorophyll a but still support water oxidation. How the FaRLiP response arose remains poorly studied. Here, we report ancestral sequence reconstruction and structure-based molecular evolutionary studies of the FRL-specific subunits of FRL-PSII. We show that the duplications leading to the origin of two PsbA (D1) paralogs required to make chlorophyll f and to bind chlorophyll d in water-splitting FRL-PSII are likely the first to have occurred prior to the diversification of extant cyanobacteria. These duplications were followed by those leading to alternative PsbC (CP43) and PsbD (D2) subunits, occurring early during the diversification of cyanobacteria, and culminating with those leading to PsbB (CP47) and PsbH paralogs coincident with the radiation of the major groups. We show that the origin of FRL-PSII required the accumulation of a relatively small number of amino acid changes and that the ancestral FRL-PSII likely contained a chlorophyll d molecule in the electron transfer chain, two chlorophyll f molecules in the antenna subunits at equivalent positions, and three chlorophyll a molecules whose site energies were altered. The results suggest a minimal model for engineering far-red light absorbance into plant PSII for biotechnological applications.

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“…The D1:Phe239 residue and Pro27 of PsbT are conserved in prokaryotic and eukaryotic PS II centers, , but although Ile29 is widely conserved in cyanobacteria, Prochlorococcus strains have Phe or Tyr at this position and green plants usually have either Ile or Val . In contrast, PsbT from C .…”

Section: Discussionmentioning

confidence: 99%

“…Utilizing the cyanobacterium Synechocystis 6803, we have previously studied the impact of removing PsbT on optimizing electron transfer through the quinone−iron acceptor complex of PS II and the sensitivity of a ΔPsbT mutant to high-light conditions. 21−23 Here we have compared the F239A and F239L mutants to a control strain, retaining the D1:Phe239 residue while possessing the kanamycin-resistance cassette employed as a selectable marker, and a ΔPsbT strain that The D1:Phe239 residue and Pro27 of PsbT are conserved in prokaryotic and eukaryotic PS II centers, 21,44 but although Ile29 is widely conserved in cyanobacteria, Prochlorococcus strains have Phe or Tyr at this position and green plants usually have either Ile or Val. 21 In contrast, PsbT from C. reinhardtii has a Met at position 29 in PsbT.…”

Section: ■ Discussionmentioning

confidence: 99%

The Interaction between PsbT and the DE Loop of D1 in Photosystem II Stabilizes the Quinone–Iron Electron Acceptor Complex

Forsman

Eaton‐Rye

2020

Biochemistry

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The X-ray-derived Photosystem II (PS II) structure from the thermophilic cyanobacterium Thermosynechococcus vulcanus (Protein Data Bank entry 4UB6) indicates Phe239 of the DE loop of the D1 protein forms a hydrophobic interaction with Pro27 and Ile29 at the C-terminus of the 5 kDa PsbT protein found at the monomer−monomer interface of the PS II dimer. To investigate the importance of this interaction, we created the F239A and F239L mutants in Synechocystis sp. PCC 6803 through targeted mutagenesis of the D1:Phe239 residue into either an alanine or a leucine. Under moderate-light conditions, the F239A strain displayed reduced rates of oxygen evolution and impaired rates of fluorescence decay following a single-turnover actinic flash, while the F239L strain behaved like the control; however, under high-light conditions, the F239A and F239L strains grew more slowly than the control. Our results indicate the quinone-iron acceptor complex becomes more accessible to exogenously added electron acceptors in the F239A mutant and a ΔPsbT strain when compared with the control and F239L strains. This led to the hypothesis that the interaction between D1:Phe239 and the PsbT subunit is required to restrict movement of the DE loop of the D1 subunit, and we suggest disruption of this interaction may perturb the binding of bicarbonate to the non-heme iron and contribute to the signal for PS II to undergo repair following photodamage.

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The diversity and distribution of D1 proteins in cyanobacteria

Cited by 28 publications

References 86 publications

Complete Genome Sequencing of a NovelGloeobacterSpecies from a Waterfall Cave in Mexico

Complete Genome Sequencing of a NovelGloeobacterSpecies from a Waterfall Cave in Mexico

Molecular Evolution of Far-Red Light-Acclimated Photosystem II

The Interaction between PsbT and the DE Loop of D1 in Photosystem II Stabilizes the Quinone–Iron Electron Acceptor Complex

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