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. 2015 May 12;43(11):5524–5536. doi: 10.1093/nar/gkv470

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — RRP1 co-fractionated and associated with the ITS2 cleavage factors in 90S particles. (A) The PR fraction was extracted and fractionated as in Figure 1B. Proteins in each fraction were analyzed by immunoblotting (IB) with the antibodies indicated at the left (top). RNAs extracted from each fraction were separated by agarose gel electrophoresis, transferred to a membrane and hybridized with the biotin-labeled probes indicated at the left (bottom). The pre-rRNA species are assigned at the right. Input: 10 μg of protein and 2 μg of RNA from each PR fraction were loaded for immunoblotting and agarose gel electrophoresis, respectively. (B) RRP1 was immunoprecipitated (IP) with anti-RRP1 from the nuclear lysate of 293T cells. Associated proteins were analyzed by immunoblotting with the antibodies indicated at the left. Normal rabbit IgG was used as a negative control for IP. The input control refers to the nuclear lysate used for IP. An asterisk indicates the presence of a non-specific band.