The plasma membrane H+-ATPases from fungi and yeasts have similar catalytic and molecular properties. A structural comparison has been performed using immunoblot analysis with polyclonal antibodies directed toward the 102 kDa polypeptide of the plasma membrane H+-ATPase from Neurospora crassa. A strong cross-reactivity is observed between the fungal H+-ATPase and the enzyme from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Structural homologies are indicated also by the analysis of the cross-reactive peptides originated by proteolytic digestion of Neurospora and S. cerevisiae purified enzymes. Neither enzyme from these two sources appears to be glycosylated by a highly sensitive concanavalin A affinity assay on blotted proteins. A glycoprotein of Mr 115000 and pI 4.8-5, which comigrates with a cell cycle-modulated protein on 2D gel, is present in partially purified preparations of plasma membrane H+-ATPase of S. cerevisiae and it is shown to be structurally unrelated to H+-ATPase.

Vai, M., Popolo, L., & Alberghina, L. (1986). Immunological cross-reactivity of fungal and yeast plasma membrane H+-ATPase. FEBS LETTERS, 206, 135-141.

Immunological cross-reactivity of fungal and yeast plasma membrane H+-ATPase

VAI, MARINA
Primo
;
ALBERGHINA, LILIA
Ultimo
1986

Abstract

The plasma membrane H+-ATPases from fungi and yeasts have similar catalytic and molecular properties. A structural comparison has been performed using immunoblot analysis with polyclonal antibodies directed toward the 102 kDa polypeptide of the plasma membrane H+-ATPase from Neurospora crassa. A strong cross-reactivity is observed between the fungal H+-ATPase and the enzyme from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Structural homologies are indicated also by the analysis of the cross-reactive peptides originated by proteolytic digestion of Neurospora and S. cerevisiae purified enzymes. Neither enzyme from these two sources appears to be glycosylated by a highly sensitive concanavalin A affinity assay on blotted proteins. A glycoprotein of Mr 115000 and pI 4.8-5, which comigrates with a cell cycle-modulated protein on 2D gel, is present in partially purified preparations of plasma membrane H+-ATPase of S. cerevisiae and it is shown to be structurally unrelated to H+-ATPase.
No
Articolo in rivista - Articolo scientifico
Scientifica
2D gel electrophoresis; Immunoblotting; H+- ATPase; Peptide mapping
English
135
141
7
Vai, M., Popolo, L., & Alberghina, L. (1986). Immunological cross-reactivity of fungal and yeast plasma membrane H+-ATPase. FEBS LETTERS, 206, 135-141.
Vai, M; Popolo, L; Alberghina, L
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/10281/99039
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