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. 2015 Apr 29;43(10):5112–5119. doi: 10.1093/nar/gkv408

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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-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 2. — Mutations in SDR5C1 affect the tRNA-maturation activities of the mtRNase P complex. (A and B) mtRNase P was reconstituted from recombinant PRORP, TRMT10C, and wild-type or mutant SDR5C1, and its activity assayed with a 5′ labeled (mt)tRNA^Ile precursor. Reaction aliquots were withdrawn and stopped at different time points and resolved by denaturing PAGE. In (A), the 1-minute time point of a representative experiment is shown. (B) Cleavage data of six complete, independent experiments were plotted as means and SD, and fit by nonlinear regression. (C and D) The methyltransferase subcomplex of mtRNase P was reconstituted from recombinant TRMT10C and wild-type or mutant SDR5C1, and its activity assayed with position-9 labeled (mt)tRNA^Ile and SAM. Reaction aliquots were withdrawn and stopped at different time points and the tRNA hydrolysate resolved by thin-layer chromatography (TLC). In (C), the 1-minute time point of a representative experiment is shown. The direction of migration and the positions of G and m¹G are indicated to the right; only the informative part of the TLC is shown. (D) Methylation data of five complete, independent experiments were plotted as means and SD, and fit by nonlinear regression.