In contrast, deletion of AGP1 in a gapl strain causes dramatic decreases in both high- and low-affinity phenylalanine uptake in MP-grown cells (Figures 1(c) and 1(d)), indicating that Agp1p is acting as the primary phenylalanine carrier in gapl strains.
Under the same experimental conditions the inhibition profiles of phenylalanine uptake are quite different in the gapl strains (Table 5) as compared to the GAP1 strains (Tables 3 and 4).
The results shown in Table 5 provide further evidence that Agp1p is an important transporter in MP-grown cells lacking GAPl. Leucine, tryptophan, and particularly asparagine compete with phenylalanine for transport.
In order to complete the proof using the characterization of PL mentioned above, we have to show that the function p is in GapL.
The reward function is part of the input too, thus r is in GapL (note that rewards may be negative integers).