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Literature summary for 7.1.2.2 extracted from

  • Hayashi, K.; Sun-Wada, G.H.; Wada, Y.; Nakanishi-Matsui, M.; Futai, M.
    Defective assembly of a hybrid vacuolar H(+)-ATPase containing the mouse testis-specific E1 isoform and yeast subunits (2008), Biochim. Biophys. Acta, 1777, 1370-1377.
    View publication on PubMed
Search for more literature for 7.1.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of a hybrid enzyme, formed by a mouse E1 isozyme and Saccharomyces cerevisiae subunits, in DELTAvma4 cells Mus musculus
expression of a hybrid enzyme, formed by a mouse E1 isozyme and yeast subunits, in DELTAvma4 cells Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits shows a defective assembly, reversible defect of the hybrid V-ATPase. Glucose depletion, known to dissociate V1 from Vo in yeast, has only a slight effect on the hybrid at acidic pH. The domain between Lys26 and Val83 of E1, which contains eight residues not conserved between E1 and E2, is responsible for the unique properties of the hybrid, while the E2 domain in E2/VMA4-2 chimera corresponding to between Lys26 and Val83 of E1 has no effect on the assembly of the V-ATPase. The mutant shows a temperature-sensitive defect Mus musculus
additional information hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits shows a defective assembly, reversible defect of the hybrid V-ATPase. Glucose depletion, known to dissociate V1 from Vo in yeast, has only a slight effect on the hybrid at acidic pH. The domain between Lys26 and Val83 of E1, which contains eight residues not conserved between E1 and E2, is responsible for the unique properties of the hybrid, while the E2 domain in E2/VMA4-2 chimera corresponding to between Lys26 and Val83 of E1 has no effect on the assembly of the V-ATPase. The mutant shows a temperature-sensitive defect Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuolar membrane
-
 Mus musculus 5774
-
vacuolar membrane
-
 Saccharomyces cerevisiae 5774
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
testis E1 isozyme Mus musculus
-

Subunits

Subunits Comment Organism
multimer
-
 Mus musculus
multimer
-
 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
V-ATPase
-
 Mus musculus
V-ATPase
-
 Saccharomyces cerevisiae
vacuolar H+-ATPase
-
 Mus musculus
vacuolar H+-ATPase
-
 Saccharomyces cerevisiae
vacuolar-type proton pumping ATPase
-
 Mus musculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 the recombinant hybrid enzyme Vo subunit a epitope is exposed to the corresponding antibody at 37 °C, but becomes inaccessible at 30 °C, showing apparent uncoupling between ATPase and proton transport Saccharomyces cerevisiae
30
-
 the recombinant hybrid enzyme Vo subunit a epitope is exposed to the corresponding antibody at 37°C, but becomes inaccessible at 30°C, showing apparent uncoupling between ATPase and proton transport Mus musculus