Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase

Li, Yunxiang; Ma, Xiaochu; Weber, Joachim

doi:10.1016/j.bbabio.2019.06.016

Cited by 6 publications

(2 citation statements)

References 56 publications

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“…Rather our data suggest that hope2 is having to 'peddle faster' to obtain the WT ATP/ADP ratio via increasing CET, as discussed above. Indeed, the C87K mutation in the Rossman fold motif of the E. coli ATP synthase γ-subunit (C139 in Arabidopsis) has been shown to decrease the coupling efficiency between the Fo rotor and F1 head, increasing the effective H + /ATP ratio (Li et al, 2019). Therefore, the G134D mutation in close proximity to this region of the protein could produce a similar effect in Arabidopsis.…”

Section: The Nature Of the Mis-regulation Of Atp Synthase In Hope2mentioning

confidence: 99%

High cyclic electron transfer via the PGR5 pathway in the absence of photosynthetic control

et al. 2023

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The light reactions of photosynthesis couple electron and proton transfers across the thylakoid membrane, generating NADPH, and proton motive force (pmf) that powers the endergonic synthesis of ATP by ATP synthase. ATP and NADPH are required for CO2 fixation into carbohydrates by the Calvin-Benson-Bassham cycle (CBBC). The dominant ΔpH component of the pmf also plays a photoprotective role in regulating photosystem II (PSII) light harvesting efficiency through non-photochemical quenching (NPQ) and photosynthetic control via electron transfer from cytochrome b6f (cytb6f) to photosystem I (PSI). ΔpH can be adjusted by increasing the proton influx into the thylakoid lumen via upregulation of cyclic electron transfer (CET) or decreasing proton efflux via downregulation of ATP synthase conductivity (gH+). The interplay and relative contributions of these two elements of ΔpH control to photoprotection are not well understood. Here, we showed that an Arabidopsis (Arabidopsis thaliana) ATP synthase mutant hunger for oxygen in photosynthetic transfer reaction 2 (hope2) with 40% higher proton efflux has supercharged CET. Double crosses of hope2 with the CET-deficient proton gradient regulation 5 and ndh-like photosynthetic complex I (ndho) lines revealed that PGR5-dependent CET is the major pathway contributing to higher proton influx. PGR5-dependent CET allowed hope2 to maintain wild-type levels of ΔpH, CO2 fixation and NPQ, however photosynthetic control remained absent and PSI was prone to photoinhibition. Therefore, high CET in the absence of ATP synthase regulation is insufficient for PSI photoprotection.

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Section: The Nature Of the Mis-regulation Of Atp Synthase In Hope2mentioning

confidence: 99%

High cyclic electron transfer via the PGR5 pathway in the absence of photosynthetic control

et al. 2023

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“…Protein concentrations were determined using the Pierce BCA Protein Assay Kit (Thermo‐Fisher, Rockford, Illinois, USA). ATPase activities were determined as reported elsewhere [41], following inorganic phosphate concentration using the malachite green phosphate assay [42] in 96‐well microplates. All peptides were previously incubated with 1.1 μ m Ec F 1 for 1 h at 30 °C, in the presence of 1 m m ATP, 1 m m Mg(II), 50 m m TRIS‐SO 4 , pH 8.0.…”

Section: Methodsmentioning

confidence: 99%

Engineering protein fragments via evolutionary and protein–protein interaction algorithms: de novo design of peptide inhibitors for F_OF₁‐ATP synthase

et al. 2020

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Enzyme subunit interfaces have remarkable potential in drug design as both target and scaffold for their own inhibitors. We show an evolution‐driven strategy for the de novo design of peptide inhibitors targeting interfaces of the Escherichia coli FoF1‐ATP synthase as a case study. The evolutionary algorithm ROSE was applied to generate diversity‐oriented peptide libraries by engineering peptide fragments from ATP synthase interfaces. The resulting peptides were scored with PPI‐Detect, a sequence‐based predictor of protein–protein interactions. Two selected peptides were confirmed by in vitro inhibition and binding tests. The proposed methodology can be widely applied to design peptides targeting relevant interfaces of enzymatic complexes.

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Chloroplast ATP synthase from green microalgae

Buchert

2020

Advances in Botanical Research

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Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase

Cited by 6 publications

References 56 publications

High cyclic electron transfer via the PGR5 pathway in the absence of photosynthetic control

High cyclic electron transfer via the PGR5 pathway in the absence of photosynthetic control

Engineering protein fragments via evolutionary and protein–protein interaction algorithms: de novo design of peptide inhibitors for F_OF₁‐ATP synthase

Chloroplast ATP synthase from green microalgae

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Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase

Cited by 6 publications

References 56 publications

High cyclic electron transfer via the PGR5 pathway in the absence of photosynthetic control

High cyclic electron transfer via the PGR5 pathway in the absence of photosynthetic control

Engineering protein fragments via evolutionary and protein–protein interaction algorithms: de novo design of peptide inhibitors for FOF1‐ATP synthase

Chloroplast ATP synthase from green microalgae

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Engineering protein fragments via evolutionary and protein–protein interaction algorithms: de novo design of peptide inhibitors for F_OF₁‐ATP synthase