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. 2016 Jul;22(7):1011–1025. doi: 10.1261/rna.056515.116

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© 2016 Chatterjee et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 8. — Purification of recombinant Mmi1 YTH domain. An alignment of the amino acid sequences of S. pombe (Spo) and S. japonicum (Sja) Mmi1 proteins is shown in panel B. Positions of side-chain identity/similarity are indicated by dots above the alignment. Gaps in the alignment are denoted by dashes. Three versions of the Mmi1 C-terminal YTH domain, extending from the Ser301, Ser311, or Ser319 sites (demarcated by arrows in panel B) to the C-terminus were produced in E. coli and purified as described in Materials and Methods. Aliquots (5 µg) of the three purified Mmi1 YTH domains were analyzed by SDS-PAGE. The Coomassie blue-stained gel is shown in panel A. The N-terminus of each YTH domain is indicated above the lane. The positions and sizes (kDa) of marker polypeptides are indicated on the left.