Purification and biochemical characterization of the ATP synthase from Heliobacterium modesticaldum

Yang, Jay How; Sarrou, Iosifina; Martín-García, José M.; Zhang, Shangji; Redding, Kevin; Fromme, Petra

doi:10.1016/j.pep.2015.05.006

Cited by 6 publications

(4 citation statements)

References 62 publications

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“…as previously described for Heliobacterium modesticaldum 55 . Five kilograms of fresh baby spinach leaves (Fresh Express, Chiquita Brands International Inc.) were stored at 4°C in the darkness for at least 3 days.…”

Section: Methodsmentioning

confidence: 99%

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Structural basis of redox modulation on chloroplast ATP synthase

et al. 2020

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In higher plants, chloroplast ATP synthase has a unique redox switch on its γ subunit that modulates enzyme activity to limit ATP hydrolysis at night. To understand the molecular details of the redox modulation, we used single-particle cryo-EM to determine the structures of spinach chloroplast ATP synthase in both reduced and oxidized states. The disulfide linkage of the oxidized γ subunit introduces a torsional constraint to stabilize the two β hairpin structures. Once reduced, free cysteines alleviate this constraint, resulting in a concerted motion of the enzyme complex and a smooth transition between rotary states to facilitate the ATP synthesis. We added an uncompetitive inhibitor, tentoxin, in the reduced sample to limit the flexibility of the enzyme and obtained high-resolution details. Our cryo-EM structures provide mechanistic insight into the redox modulation of the energy regulation activity of chloroplast ATP synthase.

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Section: Methodsmentioning

confidence: 99%

“…Samples of the chloroplast ATP synthase complexes were purified from baby spinach, Spinacia oleracea , as previously described for Heliobacterium modesticaldum 55 . Five kilograms of fresh baby spinach leaves (Fresh Express, Chiquita Brands International Inc.) were stored at 4 °C in the darkness for at least 3 days.…”

Section: Methodsmentioning

confidence: 99%

Structural basis of redox modulation on chloroplast ATP synthase

et al. 2020

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“…NativeMark Protein standard (LC0725, Invitrogen) was used as the molecular weight marker, and run with the samples. Following electrophoresis, the resulting gel was either stained with Coomassie Brilliant blue G 250 (1.15444, Sigma) or was subjected to in-gel activity assays as described below 106 , 107 . Complexes were optionally analysed on separate gel stripes or consecutively.…”

Section: Methodsmentioning

confidence: 99%

M1BP is an essential transcriptional activator of oxidative metabolism during Drosophila development

et al. 2023

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Oxidative metabolism is the predominant energy source for aerobic muscle contraction in adult animals. How the cellular and molecular components that support aerobic muscle physiology are put in place during development through their transcriptional regulation is not well understood. Using the Drosophila flight muscle model, we show that the formation of mitochondria cristae harbouring the respiratory chain is concomitant with a large-scale transcriptional upregulation of genes linked with oxidative phosphorylation (OXPHOS) during specific stages of flight muscle development. We further demonstrate using high-resolution imaging, transcriptomic and biochemical analyses that Motif-1-binding protein (M1BP) transcriptionally regulates the expression of genes encoding critical components for OXPHOS complex assembly and integrity. In the absence of M1BP function, the quantity of assembled mitochondrial respiratory complexes is reduced and OXPHOS proteins aggregate in the mitochondrial matrix, triggering a strong protein quality control response. This results in isolation of the aggregate from the rest of the matrix by multiple layers of the inner mitochondrial membrane, representing a previously undocumented mitochondrial stress response mechanism. Together, this study provides mechanistic insight into the transcriptional regulation of oxidative metabolism during Drosophila development and identifies M1BP as a critical player in this process.

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“…A single operon containing all eight genes encoding the subunits of ATP synthase (atpABCDEFGH) was identified in the genome of Hbt. modesticaldum [6,26], and the encoded ATP synthase itself has since been biochemically characterized [76]. The composition and arrangement of ATP synthase genes in Hrs.…”

Section: Reaction Center and Electron Transport Chainmentioning

confidence: 99%

Analysis of the Complete Genome of the Alkaliphilic and Phototrophic Firmicute Heliorestis convoluta Strain HHT

et al. 2020

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Despite significant interest and past work to elucidate the phylogeny and photochemistry of species of the Heliobacteriaceae, genomic analyses of heliobacteria to date have been limited to just one published genome, that of the thermophilic species Heliobacterium (Hbt.) modesticaldum str. Ice1T. Here we present an analysis of the complete genome of a second heliobacterium, Heliorestis (Hrs.) convoluta str. HHT, an alkaliphilic, mesophilic, and morphologically distinct heliobacterium isolated from an Egyptian soda lake. The genome of Hrs. convoluta is a single circular chromosome of 3.22 Mb with a GC content of 43.1% and 3263 protein-encoding genes. In addition to culture-based observations and insights gleaned from the Hbt. modesticaldum genome, an analysis of enzyme-encoding genes from key metabolic pathways supports an obligately photoheterotrophic lifestyle for Hrs. convoluta. A complete set of genes encoding enzymes for propionate and butyrate catabolism and the absence of a gene encoding lactate dehydrogenase distinguishes the carbon metabolism of Hrs. convoluta from its close relatives. Comparative analyses of key proteins in Hrs. convoluta, including cytochrome c553 and the Fo alpha subunit of ATP synthase, with those of related species reveal variations in specific amino acid residues that likely contribute to the success of Hrs. convoluta in its highly alkaline environment.

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Purification and biochemical characterization of the ATP synthase from Heliobacterium modesticaldum

Cited by 6 publications

References 62 publications

Structural basis of redox modulation on chloroplast ATP synthase

Structural basis of redox modulation on chloroplast ATP synthase

M1BP is an essential transcriptional activator of oxidative metabolism during Drosophila development

Analysis of the Complete Genome of the Alkaliphilic and Phototrophic Firmicute Heliorestis convoluta Strain HHT

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