Structural basis of redox modulation on chloroplast ATP synthase

Yang, Jay How; Williams, Dewight; Kandiah, Eaazhisai; Fromme, Petra; Chiu, Po-Lin

doi:10.1038/s42003-020-01221-8

Cited by 33 publications

(36 citation statements)

References 77 publications

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“…. Figure 3 is based on knowledge of both oxidised and reduced structures of the plant chloroplast ATP synthase [12,13].…”

Section: Regulation Of Atp Synthases In Photosynthetic Organismsmentioning

confidence: 99%

“…To understand this regulatory feature from a structural point of view, the plant chloroplast F 1 F o -ATP synthase has been recently solved by cryo -EM at high-resolution in both an oxidised (inactive) state [ 12 ] and a reduced (active) state [ 13 ]. The latter was obtained by reducing the sample with DTT and stabilising this state with the uncompetitive inhibitor, tentoxin.…”

Section: Regulation Of Atp Synthases In Photosynthetic Organismsmentioning

confidence: 99%

“…While in the light, γ Cys 240 and γ Cys 246 are reduced ( red square) and the γ -subunit does not clash with the β- DELSEED motif ( blue square). Figure 3 is based on knowledge of both oxidised and reduced structures of the plant chloroplast ATP synthase [ 12 , 13 ].…”

Section: Regulation Of Atp Synthases In Photosynthetic Organismsmentioning

confidence: 99%

“…The ATP synthase from bacterial, chloroplast and mitochondrial sources plays a key role in cellular bioenergetics and has been studied by biochemical and structural methods already for many decades [8][9][10][11]. More recently, electron cryo-microscopy (cryo-EM) has revealed the structure of fully intact F-type ATP synthases from chloroplasts at highresolution, resolving the intermediary conformational states and other key mechanistic and regulatory aspects (Figure 1) [12,13]. (A) The F 1 F o -ATP synthase from spinach chloroplast is found embedded in the thylakoid membranes and couples the proton-motive force, pmf, with the synthesis of ATP.…”

Section: Introductionmentioning

confidence: 99%

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Rotor subunits adaptations in ATP synthases from photosynthetic organisms

Cheuk

Meier

2021

Biochemical Society Transactions

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Driven by transmembrane electrochemical ion gradients, F-type ATP synthases are the primary source of the universal energy currency, adenosine triphosphate (ATP), throughout all domains of life. The ATP synthase found in the thylakoid membranes of photosynthetic organisms has some unique features not present in other bacterial or mitochondrial systems. Among these is a larger-than-average transmembrane rotor ring and a redox-regulated switch capable of inhibiting ATP hydrolysis activity in the dark by uniquely adapted rotor subunit modifications. Here, we review recent insights into the structure and mechanism of ATP synthases specifically involved in photosynthesis and explore the cellular physiological consequences of these adaptations at short and long time scales.

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“…. Figure 3 is based on knowledge of both oxidised and reduced structures of the plant chloroplast ATP synthase [12,13].…”

Section: Regulation Of Atp Synthases In Photosynthetic Organismsmentioning

confidence: 99%

Section: Regulation Of Atp Synthases In Photosynthetic Organismsmentioning

confidence: 99%

Section: Regulation Of Atp Synthases In Photosynthetic Organismsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Rotor subunits adaptations in ATP synthases from photosynthetic organisms

Cheuk

Meier

2021

Biochemical Society Transactions

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“…For a long time, the structure of this region remained unknown; however, since 2018, three papers have been published on this subject; two of them pertain to the structures of F o F 1 from the chloroplasts of Spinacea oleracea and the other describes the structure of the γ–ε subcomplex from a thermophilic cyanobacterium, Thermosynechococcus elongatus BP-1 ( T. elongatus ) ( 23 , 24 , 25 ). It was revealed that this region forms a unique β-hairpin structure that extends along the central coiled-coil stalk and interacts with the “DELSEED” loop of the β subunit ( Fig.…”

mentioning

confidence: 99%

The phototroph-specific β-hairpin structure of the γ subunit of FoF1-ATP synthase is important for efficient ATP synthesis of cyanobacteria

Kondo

Izumi

Inabe

et al. 2021

Journal of Biological Chemistry

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The F o F 1 synthase produces ATP from ADP and inorganic phosphate. The γ subunit of F o F 1 ATP synthase in photosynthetic organisms, which is the rotor subunit of this enzyme, contains a characteristic β-hairpin structure. This structure is formed from an insertion sequence that has been conserved only in phototrophs. Using recombinant subcomplexes, we previously demonstrated that this region plays an essential role in the regulation of ATP hydrolysis activity, thereby functioning in controlling intracellular ATP levels in response to changes in the light environment. However, the role of this region in ATP synthesis has long remained an open question because its analysis requires the preparation of the whole F o F 1 complex and a transmembrane proton-motive force. In this study, we successfully prepared proteoliposomes containing the entire F o F 1 ATP synthase from a cyanobacterium, Synechocystis sp. PCC 6803, and measured ATP synthesis/hydrolysis and proton-translocating activities. The relatively simple genetic manipulation of Synechocystis enabled the biochemical investigation of the role of the β-hairpin structure of F o F 1 ATP synthase and its activities. We further performed physiological analyses of Synechocystis mutant strains lacking the β-hairpin structure, which provided novel insights into the regulatory mechanisms of F o F 1 ATP synthase in cyanobacteria via the phototroph-specific region of the γ subunit. Our results indicated that this structure critically contributes to ATP synthesis and suppresses ATP hydrolysis.

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Nanoarchitectonics of Vesicle Microreactors for Oscillating ATP Synthesis and Hydrolysis

Wang,

Fei,

et al. 2024

Angewandte Chemie

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We construct a compartmentalized nanoarchitecture to regulate bioenergy level. Glucose dehydrogenase, urease and nicotinamide adenine dinucleotide are encapsulated inside through liquid‐liquid phase separation. ATPase and glucose transporter embedded in hybrid liposomes are attached at the surface. Glucose is transported and converted to gluconic acid catalyzed by glucose dehydrogenase, resulting in an outward proton gradient to drive ATPase for ATP synthesis. In parallel, urease catalyzes hydrolysis of urea to generate ammonia, which leads to an inward proton gradient to drive ATPase for ATP hydrolysis. These processes lead to a change of the direction of proton gradient, thus achieving artificial ATP oscillation. Importantly, the frequency and the amplitude of the oscillation can be programmed. The work explores nanoarchitectonics integrating multiple components to realize artificial and precise oscillation of bioenergy level.

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Structural basis of redox modulation on chloroplast ATP synthase

Cited by 33 publications

References 77 publications

Rotor subunits adaptations in ATP synthases from photosynthetic organisms

Rotor subunits adaptations in ATP synthases from photosynthetic organisms

The phototroph-specific β-hairpin structure of the γ subunit of FoF1-ATP synthase is important for efficient ATP synthesis of cyanobacteria

Nanoarchitectonics of Vesicle Microreactors for Oscillating ATP Synthesis and Hydrolysis

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