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. 2011 Aug 16;39(21):9376–9389. doi: 10.1093/nar/gkr615

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© The Author(s) 2011. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Splicing activity and specificity of APE-EndA. (A) Predicted secondary structure of A. pernix pre-tRNA^Thr1(CGU). (B) Time-dependent cleavage of A. pernix pre-tRNA^Thr1(CGU). (C) Predicted secondary structure of A. pernix pre-tRNA^Thr2 (UGU). (D) Time-dependent cleavage of A. pernix pre-tRNA^Thr2(UGU). (E) Predicted secondary structure of the BHB mini helix of A. pernix pre-tRNA ^Thr2(UGU). (F) Time-dependent cleavage of BHB mini helix. (G) Predicted secondary structure of the BHL mini helix of C. symbiosum pre-tRNA^Tyr. (H) Time-dependent cleavage of the BHL mini helix of C. symbiosum pre-tRNA^Tyr. Short arrows in (A), (C), (E) and (G) indicate the splicing sites for each pre-tRNA. Reaction mixtures were separated on 15% polyacrylamide/7 M urea gels. In each gel, ‘C’ (first lane) indicates control (no enzyme). The cleavage products are shown using schematic models at the right hand side of the gel.