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. 2019 May 11;20(9):2343. doi: 10.3390/ijms20092343

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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ONBY serves as a substrate of ONBYRS-1 and MjONBYRS. Representative in vitro aminoacylation of MjtRNA_CUA by ONBYRS-1 (44 ± 8%, n = 6, left panel) and MjONBYRS (42 ± 9%, n = 10, middle panel) with ONBY, as well as by MjTyrRS with Tyr (48 ± 12%, n = 15, right panel) analyzed by gel electrophoresis. In vitro transcribed, uncharged tRNA served as a control (-). ONBYRS-1 does not aminoacylate tRNA_CUA with tyrosine (Tyr, left panel). Aminoacyl-tRNAs (●) were detected by their slower migration compared to uncharged tRNA (○) in 6.5% acidic denaturing PAGE. tRNAs were visualized by SYBR gold staining.