High impact information on MEP3

• In contrast, MEP1 and MEP3, which are lower affinity ammonium permeases, are not required for filamentous growth [1].
• When electrophoresed on SDS-polyacrylamide gel, the Mep1 and Mep3 proteins migrate as expected from their predicted size, whereas the Mep2 protein migrates as a high-molecular-weight smear [2].
• We also show that GmSAT1 restores NH4+ uptake in the yeast mutant by interfering with the inhibition of Mep3 [3].
• We show here that, in the 26972c mutant defective in NH4+ transport, the Mep1 protein carrying an amino acid substitution in its cytoplasmic C-terminus trans-inhibits the closely related Mep3 protein [3].

Biological context of MEP3

• Saccharomyces cerevisiae possesses three related ammonium transporters, Mep1, Mep2 and Mep3, differing in their kinetic properties and in the level and regulation of their gene expression [2].

Associations of MEP3 with chemical compounds

• Protein deglycosylation with peptide-N-glycosidase F (PNGase F) indicates that, in contrast to Mep1 and Mep3, Mep2 is an asparagine-linked glycoprotein [2].

References