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. 2019 Aug 19;9:11971. doi: 10.1038/s41598-019-48357-0

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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HpRS-dependent incorporation of ncAAs 1–35 in mTFP1_TAG128. Fluorescence intensity of mTFP1 is normalized against wild-type (WT) mTFP1 (grey bar), while expression of mTFP1_TAG128 in the absence of ncAAs (−, grey bar) served as a negative control. Error bars indicate the standard deviation of three independent experiments. (A) Substrate profiles of HpRS for class I (black): ncAAs 1–14. (B) Class II (blue): ncAAs 15–17 and class IV (orange): ncAAs 28–35. (C) Class III (green): ncAAs 18–27. (D) Comparison of the aminoacylation efficiencies of HpRS (solid) and the PylRS variant (C313V, Y349F) (no fill) for ncAAs 1, 2, 10, 11, and 14.