Defective H(+)-ATPase of hygromycin B-resistant pma1 mutants fromSaccharomyces cerevisiae.

@article{Perlin1989DefectiveHO,
  title={Defective H(+)-ATPase of hygromycin B-resistant pma1 mutants fromSaccharomyces cerevisiae.},
  author={David Scott Perlin and Shannon L. Harris and Donna Seto-Young and James E Haber},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 36},
  pages={21857-64}
}
Mutations in the plasma membrane H(+)-ATPase gene (PMA1) of Saccharomyces cerevisiae that confer growth resistance to hygromycin B have been shown recently to cause a marked depolarization of whole cell membrane potential (Perlin, D. S., Brown, C. L., and Haber, J. E. (1988) J. Biol. Chem. 263, 18118-18122). In this report, the biochemical and genetic properties of H+-ATPases from four prominent hygromycin B-resistant pma1 mutants, pma1-105, pma1-114, pma1-147, and pma1-155, are described… CONTINUE READING

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Mutations in the plasma membrane H(+)-ATPase gene ( PMA1 ) of Saccharomyces cerevisiae that confer growth resistance to hygromycin B have been shown recently to cause a marked depolarization of whole cell membrane potential ( Perlin , D. S. , Brown , C. L. , and Haber , J. E. ( 1988 ) J. Biol .
DNA sequence analysis of PMA1 from strain Y55 identified 9 base pair substitutions that resulted in 6 amino acid changes in nonconserved regions when compared to the published sequence for strain S288C. Plasma membranes of three of the four pma1 mutants contained normal amounts of H(+)-ATPase ; membranes from pma1 - 155 contained enzyme at 62% of the wild - type level .
Mutations in the plasma membrane H(+)-ATPase gene ( PMA1 ) of Saccharomyces cerevisiae that confer growth resistance to hygromycin B have been shown recently to cause a marked depolarization of whole cell membrane potential ( Perlin , D. S. , Brown , C. L. , and Haber , J. E. ( 1988 ) J. Biol .
DNA sequence analysis of PMA1 from strain Y55 identified 9 base pair substitutions that resulted in 6 amino acid changes in nonconserved regions when compared to the published sequence for strain S288C. Plasma membranes of three of the four pma1 mutants contained normal amounts of H(+)-ATPase ; membranes from pma1 - 155 contained enzyme at 62% of the wild - type level .
These results are pertinent to the mechanism of vanadate - induced enzyme inhibition and suggest that Ser-368 and Pro-640 influence the affinity of the phosphate - binding site for Pi .
These results are pertinent to the mechanism of vanadate - induced enzyme inhibition and suggest that Ser-368 and Pro-640 influence the affinity of the phosphate - binding site for Pi .
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