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• W4239964887 abstract "The NH 2 -terminus of the plasma membrane H + -ATPase is one of the least conserved segments of this protein among fungi. We constructed and expressed a mutant H + -ATPase from Saccharomyces cerevisiae deleted at an internal peptide within the cytoplasmic NH 2 -terminus (D44-F116). When the enzyme was subjected to limited trypsinolysis it was digested more rapidly than wild type H + -ATPase. Membrane fractionation experiments and immunofluorescence microscopy, using antibodies against H + -ATPase showed that the mutant ATPase is retained in the endoplasmic reticulum. The pattern observed in the immunofluorescence microscopy resembled structures similar to Russell bodies (modifications of the endoplasmic reticulum membranes) recently described in yeast. When the wild type H + -ATPase was co-expressed with the mutant, wild type H + -ATPase was also retained in the endoplasmic reticulum. Co-expression of both ATPases in a wild type yeast strain was lethal, demonstrating that this is a dominant negative mutant." @default.
• W4239964887 created "2022-05-12" @default.
• W4239964887 creator A5014739415 @default.
• W4239964887 creator A5070566928 @default.
• W4239964887 date "2000-02-01" @default.
• W4239964887 modified "2023-09-30" @default.
• W4239964887 title "An NH₂-terminal deleted plasma membrane H⁺-ATPase is a dominant negative mutant and is sequestered in endoplasmic reticulum derived structures" @default.
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• W4239964887 doi "https://doi.org/10.1139/o99-071" @default.
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