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. 2017 Jun 23;114(28):E5559–E5568. doi: 10.1073/pnas.1620959114

Fig. S6.

Fig. S6.

Polymerization and GTPase activity of hGBP1 under various lipid and temperature conditions. (A and B) Time courses of hGBP1F polymer absorbance (A) and the obtained background absorbance of liposomes as a function of lipid concentration (B). Experiments were performed with 10 µM hGBP1F in the absence of liposomes (black) and in the presence of 1 mg/mL (gray), 2 mg/mL (blue), and 5 mg/mL (orange) of final lipid concentration. Polymerization was triggered upon addition of 1 mM GTP (t = 0 s). (C and D) Analysis of hGBP1F catalyzed GTP hydrolysis products GDP (C) and GMP (D) for same experiments. (EH) Nucleotide composition of the GTPase reaction performed either with 2 μM hGBP1F at 25 °C (E) and 37 °C (F) or with 2 μM hGBP1NF at 25 °C (G) and 37 °C (H) in the absence of liposomes (filled symbols) or in the presence of 0.67 mg/mL PIP2 liposomes (open symbols).