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. 2017 Nov 24;7:16291. doi: 10.1038/s41598-017-16644-3

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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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Protein-protein interaction between MiPII and MiNAGK as detected by yeast two-hybrid (from A through F) and co-immunoprecipitation (G) assays. Images A through E show yeast co-transformed with a pair of either pGBKT7-53 and pGADT7-T as a positive control (A) or pGBKT7-Lam and pGADT7-T as a negative control (B). From C through F iamges, yeast co-transformed with either pGBKT7-glnB only (C), pGBKT7-glnB and pGADT7-accB1 (D), pGBKT7-glnB and pGADT7-accB2 (E), or pGADT7-argB and pGBKT7-glnB (F). In Image G, 6 μL, 3 μL, and 5 μL of 1 M Mg²⁺, ATP, and 2-OG as marked above the panel, respectively, were added to 1 mL solution containing 200 μg and 400 μg recombinant MiPII and MiNAGK, respectively. The presence of MiNAGK bound to the Sepharose beads was subsequently analyzed by SDS-PAGE (15% acrylamide) and Coomassie blue R-250 staining. Lane M, protein molecular marker. AP, anti-MiPII polyclonal antibody. CK, only Sepharose as a control. NK, MiNAGK.