Mutations of pma-1, the Gene Encoding the Plasma Membrane H+-ATPase of Neurospora crassa, Suppress Inhibition of Growth by Concanamycin A, a Specific Inhibitor of Vacuolar ATPases*

@article{Bowman1997MutationsOP,
  title={Mutations of pma-1, the Gene Encoding the Plasma Membrane H+-ATPase of Neurospora crassa, Suppress Inhibition of Growth by Concanamycin A, a Specific Inhibitor of Vacuolar ATPases*},
  author={Emma Jean Bowman and Forest J O'Neill and Barry J. Bowman},
  journal={The Journal of Biological Chemistry},
  year={1997},
  volume={272},
  pages={14776 - 14786}
}
Concanamycin A (CCA), a specific inhibitor of vacuolar ATPases, inhibited growth of Neurospora crassa in medium adjusted to pH 7 or above. Mutant strains were selected for growth on medium containing 1.0 μm CCA. Sixty-four (of 66) mutations mapped in the region of the pma1 locus, which encodes the plasma membrane H+-ATPase. Analysis of V-ATPase activity in isolated vacuolar membranes from the mutant strains showed wild-type activity and sensitivity to CCA. In contrast, plasma membrane H+-ATPase… 
Mutations in Subunit c of the Vacuolar ATPase Confer Resistance to Bafilomycin and Identify a Conserved Antibiotic Binding Site*
TLDR
Characterization of V-ATPase activity in the four kinds of mutant strains showed that the enzyme was resistant to bafilomycinin vitro, with half-maximal inhibition obtained at 80–400 nm compared with 6.3 nm for the wild-type enzyme.
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TLDR
To understand further the mechanism of inhibition by these antibiotics and the physiological role of the enzyme in the cell, isolated mutants of the filamentous fungus Neurospora crassa that are resistant to concanamycin are isolated.
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TLDR
Inactivation of the vma-1 gene had a pronounced effect on morphology and development of the organism, supporting the hypothesis that the V-ATPase is the in vivo target of this antibiotic.
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The Bafilomycin/Concanamycin Binding Site in Subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae*
TLDR
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Characterization of a Temperature-sensitive Yeast Vacuolar ATPase Mutant with Defects in Actin Distribution and Bud Morphology*
TLDR
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Analysis of Strains with Mutations in Six Genes Encoding Subunits of the V-ATPase
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Biosynthesis and Regulation of the Yeast Vacuolar H+-ATPase
  • P. Kane
  • Biology
    Journal of bioenergetics and biomembranes
  • 1999
TLDR
The reversible disassembly of the yeast V-ATPase may be anovel regulatory mechanism that works in vivo in coordination with many other regulatory mechanisms.
Consequences of Loss of Vph1 Protein-containing Vacuolar ATPases (V-ATPases) for Overall Cellular pH Homeostasis*
TLDR
P pH measurements in early prevacuolar compartments via a pHluorin fusion to the Golgi protein Gef1 demonstrate that pH responses of these compartments parallel cytosolic pH changes, causing them to remain acidic even in the absence of V-ATPase function.
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