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. 2023 Mar 23;51(8):3988–3999. doi: 10.1093/nar/gkad192

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© The Author(s) 2023. 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 (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Arg80 and Lys50 are critical for both RNA binding and substrate deacylation. (A) Analytical ultracentrifugation sedimentation velocity analysis of 1 μM WT microhelix^Pro alone (dashed line), and in the presence of 9.6 μM WT (black), R80A (green) or K50A (blue) ProXp-ala. Inset table shows s_w values obtained from integrated c(s) distributions. (B) Single-turnover deacylation assays of 0.1 μM Ala-tRNA^Pro by 0.75 μM WT (black), R80A (green) and K50A (blue) ProXp-ala. Inset shows an expanded view of the WT and K50A ProXp-ala data. Lines represent single- (R80A) and double- (K50A and WT) exponential fits of the data. Error bars are the standard deviation of three replicates. All deacylation analyses were performed after correcting for nonenzymatic buffer hydrolysis at each timepoint.