The DbpA catalytic core unwinds double-helix substrates by directly loading on them

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FIGURE 2.
FIGURE 2.

The role of 2′-OH moieties in DbpA ATPase activity. (A) Activation of the ATPase activity of DbpA with a titration of ATP*Mg in the presence of 2000 nM of A construct (filled triangle), B construct (circle), C construct (diamond), D construct (empty square), and E construct (filled square). (B) Activation of the ATPase activity of DbpA with titrations of the A construct (filled triangle), B construct (circle), C construct (diamond), D construct (empty square), and E construct (filled square) in the presence of 5 mM ATP. The data shown represent one experiment. The average values and standard deviations for the kinetics and thermodynamic parameters obtained from fitting the Michaelis–Menten equation to similar data are shown in Table 2.

This Article

  1. RNA 22: 408-415