Molecular mechanism of regulation of yeast plasma membrane H(+)-ATPase by glucose. Interaction between domains and identification of new regulatory sites.

@article{Eraso1994MolecularMO,
  title={Molecular mechanism of regulation of yeast plasma membrane H(+)-ATPase by glucose. Interaction between domains and identification of new regulatory sites.},
  author={Pilar Eraso and Francisco Portillo},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 14},
  pages={10393-9}
}
The carboxyl terminus of yeast plasma membrane H(+)-ATPase is an autoinhibitory domain, and its effect is counteracted by modification of the enzyme triggered by glucose metabolism (Portillo, F., Larrinoa, I. F., and Serrano, R. (1989) FEBS Lett. 247, 381-385). To identify interacting domains involved in this regulation, we have performed intragenic suppressor analysis. A double mutation at the carboxyl terminus (S911A/T912A) results in no activation of the ATPase by glucose and lack of yeast… CONTINUE READING

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