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• W2108682718 endingPage "624" @default.
• W2108682718 startingPage "615" @default.
• W2108682718 abstract "ABSTRACT The gene encoding the plasma membrane proton pump (H + -ATPase) of Aspergillus fumigatus , PMA1 , was characterized from A. fumigatus strain NIH 5233 and clinical isolate H11-20. An open reading frame of 3,109 nucleotides with two introns near the N terminus predicts a protein consisting of 989 amino acids with a molecular mass of approximately 108 kDa. The predicted A. fumigatus enzyme is 89 and 51% identical to H + - ATPases of Aspergillus nidulans and Saccharomyces cerevisiae , respectively. The A. fumigatus PMA1 is a typical member of the P-type ATPase family that contains 10 predicted transmembrane segments and conserved sequence motifs TGES, CSDKTGT, MLTGD, and GDGVN within the catalytic region. The enzyme represents 2% of the total plasma membrane protein, and it is characteristically inhibited by orthovanadate, with a 50% inhibitory concentration of ∼1.8 μM. H + -ATPases from Aspergillus spp. contain a highly acidic insertion region of 60 amino acids between transmembrane segments 2 and 3, which was confirmed for the membrane-assembled enzyme with a peptide-derived antibody. An increasing A. fumigatus PMA1 copy number confers enhanced growth in low-pH medium, consistent with its role as a proton pump. These results provide support for the development of the A. fumigatus H + -ATPase as a potential drug discovery target." @default.
• W2108682718 created "2016-06-24" @default.
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• W2108682718 date "2002-03-01" @default.
• W2108682718 modified "2023-09-25" @default.
• W2108682718 title "Molecular Evaluation of the Plasma Membrane Proton Pump from<i>Aspergillus fumigatus</i>" @default.
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• W2108682718 doi "https://doi.org/10.1128/aac.46.3.615-624.2002" @default.
• W2108682718 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/127506" @default.
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