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Literature summary for 7.1.3.1 extracted from

  • Perez-Castineira, J.R.; Hernandez, A.; Drake, R.; Serrano, A.
    A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast (2011), Biochem. J., 437, 269-278.
    View publication on PubMed
Search for more literature for 7.1.3.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of AVP1, preferentially targeted to internal membranes, in Saccharomyces cerevisiae YPC3 mutant strain, generated from haploid strain W303-1A, and YPC4 mutant strain, generated from strain RS-1144 Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information expression of a chimaeric derivative of the Arabidopsis thaliana H+ -PPase AVP1, which is preferentially targeted to internal membranes of yeast, alleviates the phenotypes associated with V-ATPase deficiency. Phenotypic complementation was achieved both with a yeast strain with its V-ATPase specifically inhibited by bafilomycin A1 and with a vma1-null mutant lacking a catalytic V-ATPase subunit. Cells expressing the different AVP1 chimaeras show a somewhat smaller sensitivity to this CaCl2. In the presence of Zn2+ , only those cells transformed with plasmids pTcAVP1 and pTcGFPAVP1 expressing internal membrane-targeted chimaeras grows after 4 days, particularly the latter. Phenotypes, overview. In yeast strain YPC4, the presence of GFP at the N-terminus of AVP1 increased the specific activity of the resulting protein 3-4-fold with respect to AVP1 and TcAVP1 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Arabidopsis thaliana 16020
-
vacuole
-
 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 P31414
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane 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]
-
 ?
additional information proton-translocation activities are assayed by monitoring the fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine Arabidopsis thaliana ?
-
 ?

Subunits

Subunits Comment Organism
homooligomer
-
 Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
AVP1
-
 Arabidopsis thaliana
H+ -PPase
-
 Arabidopsis thaliana
H+ -translocating PPase
-
 Arabidopsis thaliana
inorganic pyrophosphatase
-
 Arabidopsis thaliana
single-subunit H+ -PPase
-
 Arabidopsis thaliana
V-ATPase
-
 Arabidopsis thaliana
vacuolar H+ -ATPase
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
additional information vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane Arabidopsis thaliana
physiological function vacuolar H+ -ATPases are a specific class of multisubunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. The plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance when recombinantly expressed in yeast Arabidopsis thaliana