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. 2018 Mar 20;46(7):3643–3656. doi: 10.1093/nar/gky211

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© The Author(s) 2018. 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 Non-Commercial 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 6. — SDS-PAGE analysis of purified mThrRS and mThrRS-L-N^T from Escherichia coli, editing and aminoacylation activities of ThrRSs. (A) SDS-PAGE analysis of purified mThrRS and mThrRS-L-N^T. Samples of 2 μg were loaded onto a 10% SDS-PAGE gel and stained with Coomassie Brilliant Blue. (B) Preformed Ser-tRNA^Thr was hydrolyzed by mThrRS (black square), mThrRS-H154A-H158A (white square), mThrRS-L-N^T (black inverted triangle) or mThrRS-L-N^T-H222A-H226A (white square). Spontaneous hydrolysis was measured as a negative control, by adding no enzyme (black circle). Aminoacylation of mThrRS (black square) and mThrRS-H154A-H158A (white triangle) (C) or mThrRS-L-N^T (black inverted triangle) and mThrRS-L-N^T-H222A-H226A (white diamond) (D) was compared. Data represent averages of three independent experiments and the corresponding standard errors. Some error bars are hidden by symbols.