a split-ubiquitin two-hybrid screen for proteins physically interacting with the yeast amino acid transceptor gap1 and ammonium transceptor mep2身体一个split-ubiquitin二者混合筛选蛋白质相互作用的酵母氨基酸transceptor gap1和铵transceptor mep2.pdfVIP
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a split-ubiquitin two-hybrid screen for proteins physically interacting with the yeast amino acid transceptor gap1 and ammonium transceptor mep2身体一个split-ubiquitin二者混合筛选蛋白质相互作用的酵母氨基酸transceptor gap1和铵transceptor mep2
A Split-Ubiquitin Two-Hybrid Screen for Proteins
Physically Interacting with the Yeast Amino Acid
Transceptor Gap1 and Ammonium Transceptor Mep2
Griet Van Zeebroeck1,2, Marlies Kimpe1,2, Patrick Vandormael1,2¤, Johan M. Thevelein1,2*
1 Laboratory of Molecular Cell Biology, Institute of Botany and Microbiology, KULeuven, Flanders, Belgium, 2 Department of Molecular Microbiology, The Vlaams Instituut
voor Biotechnologie, Flanders, Belgium
Abstract
Several nutrient permeases have been identified in yeast, which combine a transport and receptor function, and are
called transceptors. The Gap1 general amino acid permease and the Mep2 ammonium permease mediate rapid
activation by amino acids and by ammonium, respectively, of the protein kinase A (PKA) pathway in nitrogen-starved
cells. Their mode of action is not well understood. Both proteins are subject to complex controls governing their
intracellular trafficking. Using a split-ubiquitin yeast two-hybrid screen with Gap1 or Mep2 as bait, we identified proteins
putatively interacting with Gap1 and/or Mep2. They are involved in glycosylation, the secretory pathway, sphingolipid
biosynthesis, cell wall biosynthesis and other processes. For several candidate interactors, determination of transport and
signaling capacity, as well as localization of Gap1 or Mep2 in the corresponding deletion strains, confirmed a functional
interaction with Gap1 and/or Mep2. Also common interacting proteins were identified. Transport and signaling were
differentially affected in specific deletion strains, clearly separating the two functions of the transceptors and confirming
that signaling does not require transport. We identified two new proteins, Bsc6 and Yir014w, that affect trafficking or
downregulation of Gap1. Deletion of EGD2, YNL024c
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