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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 10. Reconstituted UTase/UR-PII cycles containing mixtures of the monofunctional altered HD-AA UTase/UR and D107N UTase/UR.

Figure 10

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 altered HD-AA UTase/UR was at 0.8 µM, and the altered D107N UTase/UR was present at 0.8 µM, 2.4 µM, 4 µM, 5.6 µM or 7.2 µM to provide the indicated ratios of enzymes. B. Glutamine signaling by reconstituted UTase/UR-PII cycles containing combination of enzymes. PII was present at 36 µM in all reactions. ■, reactions contained 0.5 µM his-tagged HD-AA UTase/UR and 2 µM D107N UTase/UR. ●, reactions contained 0.5 µM his-tagged UTase/UR (UQ5516) and 2 µM D107N UTase/UR.