ArticlePlant physiology2023
Characterization of mutants deficient in N-terminal phosphorylation of the chloroplast ATP synthase subunit β.
Article in Plant physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Deciphering the genetic basis of nodule number through integrative analysis of host genotype and endophytes.Journal of advanced research · 2026Article
- Quantitative phosphoproteomics profiling reveals the regulatory mechanisms underlying high light stress in maize and rice.Photosynthesis research · 2026Article
- Loss of qE Does Not Necessarily Lead to Photoinhibition: Sustained Non-Photochemical Quenching in the Absence of PsbS and Zeaxanthin.Plant, cell & environment · 2026Article
- Plastid Engineering for Photosynthesis-Driven Synthesis of Hyaluronic Acid in Tobacco.Plant biotechnology journal · 2026Article
- Development of chloroplast transformation for five species in the genus Nicotiana.The Plant journal : for cell and molecular biology · 2025Article
- Functional relocation of the maize chloroplast atpB gene to the nucleus restores photosynthetic competence to a gene-edited non-photosynthetic mutant.Plant biotechnology journal · 2025Article
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- Structure, Regulation, and Significance of Cyanobacterial and Chloroplast Adenosine Triphosphate Synthase in the Adaptability of Oxygenic Photosynthetic Organisms.Microorganisms · 2024Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the regulation of photosynthetic light harvesting and electron transfer is of great importance to efforts to improve the ability of the electron transport chain to supply downstream metabolism. A central regulator of the electron transport chain is ATP synthase, the molecular motor that harnesses the chemiosmotic potential generated from proton-coupled electron transport to synthesize ATP. ATP synthase is regulated both thermodynamically and post-translationally, with proposed phosphorylation sites on multiple subunits. In this study we focused on two N-terminal serines on the catalytic subunit β in tobacco (Nicotiana tabacum), previously proposed to be important for dark inactivation of the complex to avoid ATP hydrolysis at night. Here we show that there is no clear role for phosphorylation in the dark inactivation of ATP synthase. Instead, mutation of one of the two phosphorylated serine residues to aspartate to mimic constitutive phosphorylation strongly decreased ATP synthase abundance. We propose that the loss of N-terminal phosphorylation of ATPβ may be involved in proper ATP synthase accumulation during complex assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.