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Literature summary for 7.1.3.1 extracted from

  • Ferjani, A.; Segami, S.; Horiguchi, G.; Muto, Y.; Maeshima, M.; Tsukaya, H.
    Keep an eye on PPi: the vacuolar-type H+-pyrophosphatase regulates postgerminative development in Arabidopsis (2011), Plant Cell, 23, 2895-2908.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
A553T naturally occuring point mutation A553T plus deletion of residues from Leu554 to Ala558 in the transmembrane domain 12. The mutant fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5 Arabidopsis thaliana
A709T the naturally occuring fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to a point mutation A709T and fails to support heterotrophic growth after germination. Cell division is almost totally inhibited in cotyledons postembryonically, phenotype, overview, fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5 Arabidopsis thaliana
E272K naturally occuring point mutation, fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuole vacuolar H+-pyrophosphatase Arabidopsis thaliana 5773
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O + H+[side 1] Arabidopsis thaliana
-
2 phosphate + H+[side 2]
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana A8MQH1
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
Arabidopsis thaliana
-
leaf
-
Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O + H+[side 1]
-
Arabidopsis thaliana 2 phosphate + H+[side 2]
-
?

Synonyms

Synonyms Comment Organism
AVP1
-
Arabidopsis thaliana
V-PPase
-
Arabidopsis thaliana
vacuolar H+-pyrophosphatase
-
Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction the fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to point mutations A709T, A553T, or E272K, and fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic diphosphatase1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5 Arabidopsis thaliana
physiological function vacuolar H+-diphosphatase, AVP1, is a key enzyme in phosphate hydrolysis Arabidopsis thaliana