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. 2022 Nov 8;13:6732. doi: 10.1038/s41467-022-34612-y

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© The Author(s) 2022

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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Fig. 2 — a Close-up view of the interface between EARS1 and IARS1 UBX2. b, c Close-up view of the interaction between the EARS1 hairpin loop and IARS1 UBX domains. Mutated residues in the pull-down analysis are indicated by red boxes. a–c Color schemes are same as those in Fig. 1d. H-bonds and ion-pairs are shown in black dots. d Structure-based sequence alignments of EARS1 and QARS1 orthologs. The secondary structure of GgEARS1 is displayed on top of the sequences. IARS1-contacting residues are indicated by blue circles. Every tenth residue is marked with a black dot. e In vitro pull-down assay of GgEARS1 and the IARS1 UNE-I domain. His-GgEARS1 or His-GgEARS1Δhairpin was pulled down with Ni-NTA resin, and co-precipitated GST-GgIARS1 was detected by Coomassie staining. Black and red arrowheads indicate eluted His-GgEARS1 and GST-GgIARS1, respectively. f Incorporation of EPRS1 phosphomimetic mutants into the MSC. Flag-tagged, full-length EPRS1 wild-type protein and the phosphomimetic (Ser-to-Glu, S-E) mutant were expressed in HEK293T cells by transient transfection. Lysates were immunoprecipitated with an anti-Flag antibody, and co-precipitated IARS1 or LARS1 was detected by immunoblotting with an anti-IARS1 or anti-LARS1 antibody. g Wild-type or phosphomimetic mutant His-GgEARS1 was pulled down with Ni-NTA resin, and co-precipitated GST-GgIARS1 was detected by Coomassie staining. Black and red arrowheads indicate eluted His-GgEARS1 and GST-GgIARS1, respectively. e–g The data are representative of three independent experiments. Source data are provided as a Source Data file.