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. Author manuscript; available in PMC: 2013 Nov 13.
Published in final edited form as: Biochemistry. 2012 Nov 1;51(45):9032–9044. doi: 10.1021/bi3005736

Figure 3. A combination of his-tagged UTase/UR and an altered form of the enzyme displaying only UR activity effectively regulated PII uridylylation state in response to glutamine.

Figure 3

A. Steady state PII uridylylation state in the absence of glutamine (filled bars) and in the presence of 10 mM glutamine (unfilled bars). PII was at 36 µM, his-tagged UTase/UR (UQ5516) was at 0.5 µM, and the altered D107N UTase/UR was present at 0 µM, 0.5 µM, 1 µM, 2 µM or 3 µM to provide the indicated ratios of enzymes. B. Glutamine signaling by a reconstituted UTase/UR-PII cycle containing a combination of his-tagged UTase/UR (UQ5516) (0.5 µM) and the altered D107N UTase/UR (3 µM). PII was present at 36 µM.