ArticleFrontiers in plant science2016
Contribution of PPi-Hydrolyzing Function of Vacuolar H(+)-Pyrophosphatase in Vegetative Growth of Arabidopsis: Evidenced by Expression of Uncoupling Mutated Enzymes.
Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 38 citations in OpenAlex.
- Contrasting roles of reactive oxygen species in pyrophosphate-induced growth inhibition under normal and salt stress conditions.Plant molecular biology · 2025Article
- Marker-Assisted Backcross Breeding of Drought-Tolerant Maize Lines Transformed by Vacuolar HPlants (Basel, Switzerland) · 2025Article
- Root and Leaf Anatomy, Ion Accumulation, and Transcriptome Pattern under Salt Stress Conditions in Contrasting Genotypes ofPlants (Basel, Switzerland) · 2023Article
- Mutations in type II Golgi-localized proton pyrophosphataseFrontiers in plant science · 2023Article
- Roles of type II HFrontiers in plant science · 2023Article
- Leaf-size control beyond transcription factors: Compensatory mechanisms.Frontiers in plant science · 2022Review
- Tissue-targeted inorganic pyrophosphate hydrolysis in aFrontiers in plant science · 2022Article
- An auxin signaling network translates low-sugar-state input into compensated cell enlargement in the fugu5 cotyledon.PLoS genetics · 2021Article
- Assessment of sugar and sugar accumulation-related gene expression profiles reveal new insight into the formation of low sugar accumulation trait in a sweet orange (Citrus sinensis) bud mutant.Molecular biology reports · 2020Article
- Excess Pyrophosphate Restrains Pavement Cell Morphogenesis and Alters Organ Flatness inFrontiers in plant science · 2020Article
- Lack of Vacuolar HFrontiers in plant science · 2020Article
- Article
- The Function of Membrane Integral Pyrophosphatases From Whole Organism to Single Molecule.Frontiers in molecular biosciences · 2019Review
- Pyrophosphate inhibits gluconeogenesis by restricting UDP-glucose formation in vivo.Scientific reports · 2018Article
- Protein Phosphatase (International journal of molecular sciences · 2018Article
- Vacuolar HThe Plant cell · 2018Article
- The Phosphate Fast-Responsive GenesPlant physiology · 2018Article
- Article
- Structural basis for the reversibility of proton pyrophosphatase.Plant signaling & behavior · 2016Article
- Lack of H(+)-pyrophosphatase Prompts Developmental Damage in Arabidopsis Leaves on Ammonia-Free Culture Medium.Frontiers in plant science · 2016Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vacuolar-type H(+)-pyrophosphatase (H(+)-PPase) catalyzes a coupled reaction of pyrophosphate (PPi) hydrolysis and active proton translocation across the tonoplast. Overexpression of H(+)-PPase improves growth in various plant species, and loss-of-function mutants (fugu5s) of H(+)-PPase in Arabidopsis thaliana have post-germinative developmental defects. Here, to further clarify the physiological significance of this important enzyme, we newly generated three varieties of H(+)-PPase overexpressing lines with different levels of activity that we analyzed together with the loss-of-function mutant fugu5-3. The H(+)-PPase overexpressors exhibited enhanced activity of H(+)-PPase during vegetative growth, but no change in the activity of vacuolar H(+)-ATPase. Overexpressors with high enzymatic activity grew more vigorously with fresh weight increased by more than 24 and 44%, compared to the wild type and fugu5-3, respectively. Consistently, the overexpressors had larger rosette leaves and nearly 30% more cells in leaves than the wild type. When uncoupling mutated variants of H(+)-PPase, that could hydrolyze PPi but could not translocate protons, were introduced into the fugu5-3 mutant background, shoot growth defects recovered to the same levels as when a normal H(+)-PPase was introduced. Taken together, our findings clearly demonstrate that additional expression of H(+)-PPase improves plant growth by increasing cell number, predominantly as a consequence of the PPi-hydrolyzing activity of the enzyme.
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