A Split-Ubiquitin Two-Hybrid Screen for Proteins Physically Interacting with the Yeast Amino Acid Transceptor Gap1 and Ammonium Transceptor Mep2
2011

Identifying Proteins Interacting with Yeast Amino Acid Transceptors

publication Evidence: moderate

Author Information

Author(s): Van Zeebroeck Griet, Kimpe Marlies, Vandormael Patrick, Thevelein Johan M.

Primary Institution: Laboratory of Molecular Cell Biology, Institute of Botany and Microbiology, KULeuven, Flanders, Belgium

Hypothesis

The study aims to identify proteins that interact with the yeast amino acid transceptors Gap1 and Mep2 using a split-ubiquitin two-hybrid screen.

Conclusion

The study successfully identified several candidate proteins that interact with Gap1 and Mep2, revealing insights into their transport and signaling functions.

Supporting Evidence

  • The study identified proteins involved in glycosylation and cell wall biosynthesis that interact with Gap1 and Mep2.
  • Functional interactions were confirmed for several candidate proteins through deletion strain analysis.
  • Transport and signaling functions of the transceptors were shown to operate independently.

Takeaway

Researchers found new proteins that help yeast cells transport and signal nutrients, which is important for their growth.

Methodology

The study used a split-ubiquitin yeast two-hybrid system to screen for proteins interacting with Gap1 and Mep2.

Limitations

The screen may not identify interactors that require specific post-translational modifications or are only expressed under nitrogen starvation conditions.

Digital Object Identifier (DOI)

10.1371/journal.pone.0024275

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