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. 2017 Aug 31;45(19):11341–11355. doi: 10.1093/nar/gkx764

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© The Author(s) 2017. 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. — Lack of Trm1p modification at G26 results in likely misfolding of tRNA-Ser^CGA/UGA. Acid-northern (A) and periodate oxidation/β-elimination (B) to assay charging levels of various tRNA species indicates a Sla1p/Trm1p associated tRNA charging defect for tRNA-Ser^CGA/UGA. (C) Reverse transcriptase primer extension of recombinant Trm1p-modified tRNA-Phe^GAA confirms specific modification of G26 in vitro. (D) Left: lead acetate chemical probing indicates altered structure in the anticodon stem loop and variable arm of pre-tRNA-Ser^UGA after in vitro modification with Trm1p. Right: secondary structure of tRNA-Ser^UGA. Nucleotides with altered chemical reactivity to lead acetate probing +/− Trm1p modification indicated in bold. Bottom: quantitated differential lead acetate reactivity +/− Trm1p modification.