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. 2017 Jul 21;7:6135. doi: 10.1038/s41598-017-06415-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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M. tuberculosis RpsA interacts with polyC RNA, but not with POA. Isothermal titration calorimetry was used to assess the binding between RpsA and either polyC RNA (A) or POA (B). In each plot, the top panel represents the heat produced per injection as µcal/sec while the bottom panel shows the change in enthalpy (kcal/mole) as a function of the molar ratio of the two ligands. Titrations were performed at 25 °C using 10 mM phosphate buffer (pH 7.4). POA and polyC RNA solutions were adjusted to pH 7.4.