
3′-terminal uridine is specifically recognized through the ribose 2′- and 3′-OH groups when RNA is bound by the N. meningitidis ProQ protein. (A) The fitting of the ProQ binding data using the quadratic equation provided Kd values of 0.6 nM for rpmG-35, while the binding of rpmG-dU, rpmG-P, and rpmG-C did not reach saturation up to 50 nM concentration of the ProQ. The binding of rpmG-ddC was essentially undetectable up to 50 nM concentration of the ProQ. (B) The fitting of the ProQ binding data using the quadratic equation provided Kd values of 4.5 nM for AniS-37 and 10.5 nM for AniS-C, while the binding for AniS-dU, AniS-P, and AniS-ddC was essentially undetectable up to 50 nM concentration of the ProQ. The data in the plots for rpmG-35 and AniS-37 binding to ProQ are the same as in Figure 3. Gels corresponding to the data in the plots are shown in Supplemental Figure S10. The average equilibrium dissociation constant (Kd) values and maximum RNA fraction bound calculated from at least three independent experiments are shown in Table 5.










