Substitutions of aspartate 378 in the phosphorylation domain of the yeast PMA1 H+-ATPase disrupt protein folding and biogenesis.

@article{Nakamoto1998SubstitutionsOA,
  title={Substitutions of aspartate 378 in the phosphorylation domain of the yeast PMA1 H+-ATPase disrupt protein folding and biogenesis.},
  author={Robert K. Nakamoto and Sergio Verjovski-Almeida and Kenneth E. Allen and A Ambesi and Rajini Rao and Carolyn W. Slayman},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 13},
  pages={7338-44}
}
There is strong evidence that Asp-378 of the yeast PMA1 ATPase plays an essential role in ATP hydrolysis by forming a covalent beta-aspartyl phosphate reaction intermediate. In this study, Asp-378 was replaced by Asn, Ser, and Glu, and the mutant ATPases were expressed in a temperature-sensitive secretion-deficient strain (sec6-4) that allowed their properties to be examined. Although all three mutant proteins were produced at nearly normal levels and remained stable for at least 2 h at 37… CONTINUE READING

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The Molecular and Cellular Biology of the Yeast Saccharomyces: Genome Dynamics, Protein Synthesis, and Energetics

  • R. Serrano
  • 1991

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