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. 2017 Nov 27;8:1787. doi: 10.1038/s41467-017-01786-9

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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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Fig. 1 — In vitro assay for 7S→5.8S pre-rRNA processing in purified pre-60S particles catalysed by the TAP-purified nuclear exosome and cofactors. a Analysis of the protein samples used for the in vitro 7S→5.8S pre-rRNA-processing reaction. Substrate 7S pre-rRNA was part of the pre-60S particles affinity-purified via TAPF-Nop53. Endogenous yeast exosome was affinity-purified via Rrp6-FTpA, and recombinant yeast Mtr4, either wt or the K176A mutant, was expressed and affinity-purified from E. coli. The indicated eluates were analysed by SDS-PAGE and Coomassie staining. Marked bands of the exosome were identified by mass spectrometry. b Northern blot for the detection of 7S pre-rRNA, 5.8S rRNA and 5S rRNA species after the in vitro processing reaction. Processing of 7S pre-rRNA from pre-60S particles (TAPF-Nop53) using the endogenous yeast-derived nuclear exosome (FTpA-Rrp6) and its cofactor Mtr4, either wt or K176A mutant, in the presence or absence of ATP. 7S pre-rRNA was detected with two different probes. 5S rRNA served as a loading control