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. 2015 Feb 10;43(4):2400–2411. doi: 10.1093/nar/gkv072

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — The effects of Hfq mutations (N28A, K31A and N48A) on RNA binding affinities. (A) N28A (magenta), N48A (blue) and K31A (green) mutations dramatically decrease the binding affinity for A₇ to Hfq (compared with a K_d of ∼113 nM for wild-type Hfq; (19)). (B) The binding affinity of A_us RNA for N28A and K31A is both lower compared with that for wild type. In contrary, the N48A mutant exhibits higher affinity for A_us. (C) The N48A mutation dramatically increases the affinity for A_ds (∼16-fold) compared with wild type. (D) The binding affinity A_ds for the K31A mutant is significantly lower. The N28A mutation does not affect the binding of A_ds. In EMSA assays, compared to wild-type Hfq (E), the N48A mutant caused a prominent mobility shift of full-length OxySU8 at lower concentrations (F).