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. 2017 Apr 12;7:858. doi: 10.1038/s41598-017-00980-5

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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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Hfq-Crc proteins form a stable ribonucleoprotein complex with CrcZ. Ribonucleoprotein complexes formed in the presence of the sRNA CrcZ and increasing concentrations of Hfq (0, 0.02, 0.05, 0.1, 0.2, 0.5 and 1 µM) (a) or in the presence of both Crc and Hfq (b and c). In (d) Crc was substituted by 1 µM of bovine serum albumin (BSA). Crc and Hfq were added at the indicated concentrations (expressed as monomers and hexamers respectively). RNA and protein-RNA complexes were resolved in a non-denaturing polyacrylamide gel. The position of free RNA, and of the ribonucleoprotein (RNP) complexes detected, is indicated.