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. 2024 Apr 23;10(5):1044–1053. doi: 10.1021/acscentsci.3c01366

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© 2024 The Authors. Published by American Chemical Society

Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).

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MaPylRS andMaFRSA acylate tRNA^Pyl with β²-hydroxy acid substrates in vitro. (A) Workflow for and (B) deconvoluted mass spectra of in vitro tRNA^Pyl acylation reactions containing 12.5 μM MaFRSA and supplemented with monomers 1–4. Signal is normalized to the highest signal in the respective traces. Expected masses shown correspond to monoacylated products. (C) Plot illustrating the relative yields of mono- and diacylated tRNA^Pyl generated during in vitro acylation reactions containing 12.5 μM PylRS and supplemented with 10 mM of monomer 1, 2, 3, or 4. (D) Plot illustrating yield of monoacylated tRNA^Pyl as a function of [MaPylRS]. The analogous plot showing the yield of mono- + diacylated tRNA^Pyl as a function of [MaPylRS] is shown in Supporting Information Figure 2. (E) Deconvoluted mass spectra of in vitro tRNA^Pyl acylation reactions containing 12.5 μM MaFRSA and supplemented with monomers 5–8. Signal is normalized to the highest signal in respective traces. Expected masses shown correspond to monoacylated products. Control tRNA^Pyl acylation reactions in which tRNA^Pyl, enzyme, or substrate is omitted are shown in Supporting Information Figures 1 and 3.