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. 2019 Jun 13;10:2617. doi: 10.1038/s41467-019-10496-3

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© The Author(s) 2019

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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Fig. 8 — Dimeric organization of MjaRNase P. a The loops between stems P2 and P4 from the two RPRs staggered pack together. The two loops are colored in green and the two RPRs in pink and gray, respectively. The EM density map is shown in light blue mesh. b Overall view of the dimeric conformation mediated by the (Pop5-Rpp30)₂ heterotetramer. Rpp30 simultaneously interacts with the two RPR molecules in the dimeric holoenzyme. c SEC profiles of the WT (Dimer, blue) and mutant (Monomer, red) MjaRNase P complexes. d Selected 2D class averages of the WT (Dimer, top) and mutant (Monomer, bottom) MjaRNase P complexes. e In vitro tRNA processing assay of WT (Dimer) and mutant (Monomer) MjaRNase P complexes