Table 4.

Equilibrium binding of wt RNAs and their variants with mutations in the A-rich motifs to the ProQ NTD and the Hfq protein

	K d [nM]
32P-RNA	NTDa	Hfqb
malM-3′	12 ± 4.8c	22 ± 7
malM-3′-AtoU	5.0 ± 1.8	2.2 ± 0.8
cspE-3′	4.5 ± 1.5c	5.9 ± 2.5
cspE-3′-AtoU	100 ± 51	1.7 ± 0.88
cspE81-3′	7.6 ± 4.5	47 ± 11
cspE81-3′-AtoU	17 ± 4.6	2.6 ± 1.2
cspA-3′	33 ± 10d	49 ± 15d
cspA-3′-RtoU	42 ± 18d	1.3 ± 0.66
hupB-3′	18 ± 1.7	30 ± 16d
hupB-3′-RtoU	29 ± 7.2	1.9 ± 0.75
infA-3′	19 ± 10	28 ± 12d
infA-3′-AtoU	32 ± 13	1.2 ± 0.55

The K_d values were obtained by fitting the data to the quadratic equation. The average K_d values with standard deviations were calculated from three to five independent experiments, except for malM-3′ binding to the NTD (eleven replicates) and Hfq (six replicates) and cspE-3′ binding to the NTD (seven replicates) and Hfq (seven replicates).

^aThe RNA binding to the NTD was measured using gelshift assay

^bThe RNA binding to the Hfq protein was measured using double-filter retention assay

^cData from Table 1.

^dThe endpoint value of 100% was assumed in the data fitting.