Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site.

@article{Bowman2002MutationsIS,
  title={Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site.},
  author={Barry J. Bowman and Emma Jean Bowman},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 6},
  pages={
          3965-72
        }
}
Bafilomycin A1, a potent inhibitor of vacuolar H(+)-ATPases (V-ATPase), inhibited growth of Neurospora crassa in medium adjusted to alkaline pH. Ninety-eight mutant strains were selected for growth on medium (pH 7.2) containing 0.3 or 1.0 microm bafilomycin. Three criteria suggested that 11 mutant strains were altered in the V-ATPase: 1) these strains accumulated high amounts of arginine when grown at pH 5.8 in the presence of bafilomycin, 2) the mutation mapped to the locus of vma-3, which… CONTINUE READING

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