Figures
The images for Figs 4 and 5 are incorrectly switched. The image that appears as Fig 4 should be Fig 5, and the image that appears as Fig 5 should be Fig 4. The figure captions appear in the correct order. Please see the corrected Fig 4 and Fig 5 below.
Hexahistidine-tagged VvRraA1, VvRraA1-C9D, VvRraA2, VvRraA2-C9D, and the GST-fused VvRne (612–816 residues) were expressed and purified as described in the Methods section. The GST-fused VvRne protein was bound to GSH resin and incubated with VvRraA proteins and their C9D mutant proteins. Then, the proteins were eluted and the fractions were analyzed using SDS-PAGE. The protein bands were stained with Coomassie blue. Only VvRraA1 could tightly bind to VvRne.
0.5 pmol of 5’-end-labeled p-BR10+hpT RNA was incubated with 1 pmol of VvRne with varying concentrations of VvRraA1 and VvRraA1-C9D, 50 pmol of VvRraA1, or 50 pmol of BSA in 20 μl of 1 × cleavage buffer at 37°C for 2 h for VvRne, VvRraA1 only, or BSA only controls. Samples were mixed with an equal volume of loading buffer, and then denatured at 65°C for 5 min and loaded onto a 12% polyacrylamide gel containing 8 M urea. The percentage of uncleaved p-BR10+hpT in the gel was quantitated using a phosphorimager and OptiQuant software.
Reference
- 1. Song S, Hong S, Jang J, Yeom J- H, Park N, Lee J, et al. (2017) Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus. PLoS ONE 12(12): e0190064. https://doi.org/10.1371/journal.pone.0190064 pmid:29261778
Citation: Song S, Hong S, Jang J, Yeom J-H, Park N, Lee J, et al. (2018) Correction: Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus. PLoS ONE 13(1): e0191775. https://doi.org/10.1371/journal.pone.0191775
Published: January 19, 2018
Copyright: © 2018 Song et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.