The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex.

@article{Ohira2006TheEA,
  title={The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex.},
  author={Masashi Ohira and Anne M. Smardon and Colleen M H Charsky and Jianzhong Liu and Maureen Tarsio and Patricia M Kane},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 32},
  pages={22752-60}
}
The E and G subunits of the yeast V-ATPase are believed to be part of the peripheral or stator stalk(s) responsible for physically and functionally linking the peripheral V1 sector, responsible for ATP hydrolysis, to the membrane V0 sector, containing the proton pore. The E and G subunits interact tightly and specifically, both on a far Western blot of yeast vacuolar proteins and in the yeast two-hybrid assay. Amino acids 13-79 of the E subunit are critical for the E-G two-hybrid interaction… CONTINUE READING