ArticleScientific reports2017
Acetylation and phosphorylation control both local and global stability of the chloroplast F
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- Loss of Chloroplast GNAT Acetyltransferases Results in Distinct Metabolic Phenotypes in Arabidopsis.Plant & cell physiology · 2023Article
- Development of multivalent vaccine targeting M segment of Crimean Congo Hemorrhagic Fever Virus (CCHFV) using immunoinformatic approaches.Saudi journal of biological sciences · 2022Article
- Advances in proteome-wide analysis of plant lysine acetylation.Plant communications · 2022Review
- Polymorphism in the Chloroplast ATP Synthase Beta-Subunit Is Associated with a Maternally Inherited Enhanced Cold Recovery in Cucumber.Plants (Basel, Switzerland) · 2021Article
- Two Chloroplast Proteins Negatively Regulate Plant Drought Resistance Through Separate Pathways.Plant physiology · 2020Article
- Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry.Journal of visualized experiments : JoVE · 2018Article
- Chloroplast Acetyltransferase NSI Is Required for State Transitions inThe Plant cell · 2018Article
- Improved chloroplast energy balance during water deficit enhances plant growth: more crop per drop.Journal of experimental botany · 2018Article
- Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies.Journal of visualized experiments : JoVE · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
ATP synthases (ATPases) are enzymes that produce ATP and control the pH in the cell or cellular compartments. While highly conserved over different species, ATPases are structurally well-characterised but the existence and functional significance of many post-translational modifications (PTMs) is not well understood. We combined a range of mass spectrometric techniques to unravel the location and extent of PTMs in the chloroplast ATP synthase (cATPase) purified from spinach leaves. We identified multiple phosphorylation and acetylation sites and found that both modifications stabilise binding of ε and δ subunits. Comparing cross-linking of naturally modified cATPase with the in vitro deacetylated enzyme revealed a major conformational change in the ε subunit in accord with extended and folded forms of the subunit. Locating modified residues within the catalytic head we found that phosphorylated and acetylated residues are primarily on α/β and β/α interfaces respectively. By aligning along different interfaces the higher abundance acetylated residues are proximal to the regulatory sites while the lower abundance phosphorylation sites are more densely populated at the catalytic sites. We propose that modifications in the catalytic head, together with the conformational change in subunit ε, work in synergy to fine-tune the enzyme during adverse conditions.
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Registered trials
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