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. Author manuscript; available in PMC: 2014 May 27.
Published in final edited form as: J Mol Biol. 2013 Feb 14;425(10):1655–1669. doi: 10.1016/j.jmb.2013.02.010

Table 3. Kinetic profiles of reported high-affinity ETS-DNA interactions.

The values excerpted from the literature are for a construct most closely corresponding to the minimal ETS domains (i.e., minus autoinhibitory modules) that represent an appropriate counterpart to the PU.1 ETS domain. In cases where no error is stated in the table, none was reported.

ETS domain ka, M−1 s−1 kA, s−1 KD, nM [salt], mM Reference
PU.1 (3.2 ±0.1) × 104 (5.9 ±0.2) × 10−4 18 ± 1.5 250 (Na+) This work
(4.9 ± 1.2) × 105 (8.5 ± 2.0) × 10−2 170 ± 5 650 (Na+) Pióet al.21a
Ets-1 14 × 108 1.6 × 10−2 0.0085 ± 0.0007 65 (K+) + 6 Mg2+ Jonsen et al.42b
TEL (ETV6) 8.7 × 107 ~0.2 2.3 ± 0.4 50 (K+) + 6 (Mg2+) Green et al.41b
a

No nonspecific DNA was used in this SPR study.

b

kd determined by EMSA; ka inferred by Equation 4.