Vacuolar H+-Pyrophosphatase and Cytosolic Soluble Pyrophosphatases Cooperatively Regulate Pyrophosphate Levels in Arabidopsis thaliana. Issue 5 (24th April 2018)
- Record Type:
- Journal Article
- Title:
- Vacuolar H+-Pyrophosphatase and Cytosolic Soluble Pyrophosphatases Cooperatively Regulate Pyrophosphate Levels in Arabidopsis thaliana. Issue 5 (24th April 2018)
- Main Title:
- Vacuolar H+-Pyrophosphatase and Cytosolic Soluble Pyrophosphatases Cooperatively Regulate Pyrophosphate Levels in Arabidopsis thaliana
- Authors:
- Segami, Shoji
Tomoyama, Takaaki
Sakamoto, Shingo
Gunji, Shizuka
Fukuda, Mayu
Kinoshita, Satoru
Mitsuda, Nobutaka
Ferjani, Ali
Maeshima, Masayoshi - Abstract:
- Abstract : Vacuolar H + -pyrophosphatase and cytosolic soluble pyrophosphatases play the leading and supportive role, respectively, in PPi homeostasis in Arabidopsis. Abstract: Inorganic pyrophosphate (PPi) is a phosphate donor and energy source. Many metabolic reactions that generate PPi are suppressed by high levels of PPi. Here, we investigated how proper levels of cytosolic PPi are maintained, focusing on soluble pyrophosphatases (AtPPa1 to AtPPa5; hereafter PPa1 to PPa5) and vacuolar H + -pyrophosphatase (H + -PPase, AtVHP1/FUGU5) in Arabidopsis thaliana . In planta, five PPa isozymes tagged with GFP were detected in the cytosol and nuclei. Immunochemical analyses revealed a high abundance of PPa1 and the absence of PPa3 in vegetative tissue. In addition, the heterologous expression of each PPa restored growth in a soluble PPase-defective yeast strain. Although the quadruple knockout mutant plant ppa1 ppa2 ppa4 ppa5 showed no obvious phenotypes, H + -PPase and PPa1 double mutants ( fugu5 ppa1 ) exhibited significant phenotypes, including dwarfism, high PPi concentrations, ectopic starch accumulation, decreased cellulose and callose levels, and structural cell wall defects. Altered cell arrangements and weakened cell walls in the root tip were particularly evident in fugu5 ppa1 and were more severe than in fugu5 . Our results indicate that H + -PPase is essential for maintaining adequate PPi levels and that the cytosolic PPa isozymes, particularly PPa1, prevent increasesAbstract : Vacuolar H + -pyrophosphatase and cytosolic soluble pyrophosphatases play the leading and supportive role, respectively, in PPi homeostasis in Arabidopsis. Abstract: Inorganic pyrophosphate (PPi) is a phosphate donor and energy source. Many metabolic reactions that generate PPi are suppressed by high levels of PPi. Here, we investigated how proper levels of cytosolic PPi are maintained, focusing on soluble pyrophosphatases (AtPPa1 to AtPPa5; hereafter PPa1 to PPa5) and vacuolar H + -pyrophosphatase (H + -PPase, AtVHP1/FUGU5) in Arabidopsis thaliana . In planta, five PPa isozymes tagged with GFP were detected in the cytosol and nuclei. Immunochemical analyses revealed a high abundance of PPa1 and the absence of PPa3 in vegetative tissue. In addition, the heterologous expression of each PPa restored growth in a soluble PPase-defective yeast strain. Although the quadruple knockout mutant plant ppa1 ppa2 ppa4 ppa5 showed no obvious phenotypes, H + -PPase and PPa1 double mutants ( fugu5 ppa1 ) exhibited significant phenotypes, including dwarfism, high PPi concentrations, ectopic starch accumulation, decreased cellulose and callose levels, and structural cell wall defects. Altered cell arrangements and weakened cell walls in the root tip were particularly evident in fugu5 ppa1 and were more severe than in fugu5 . Our results indicate that H + -PPase is essential for maintaining adequate PPi levels and that the cytosolic PPa isozymes, particularly PPa1, prevent increases in PPi concentrations to toxic levels. We discuss fugu5 ppa1 phenotypes in relation to metabolic reactions and PPi homeostasis. … (more)
- Is Part Of:
- The Plant Cell. Volume 30:Issue 5(2018)
- Journal:
- The Plant Cell
- Issue:
- Volume 30:Issue 5(2018)
- Issue Display:
- Volume 30, Issue 5 (2018)
- Year:
- 2018
- Volume:
- 30
- Issue:
- 5
- Issue Sort Value:
- 2018-0030-0005-0000
- Page Start:
- 1040
- Page End:
- 1061
- Publication Date:
- 2018-04-24
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.17.00911 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 19591.xml