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. 2017 Jul 31;8:159. doi: 10.1038/s41467-017-00188-1

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© The Author(s) 2017

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. 4 — The mutations of Rqt2 in the conserved residues in ATPase domain diminished RQC. a Alignment of the conserved residues in the RecA1 motif I of Slh1/Rqt2, Brr2, Ski2, and hRad51. The substitution of the lysine to arginine residue of motif I in human Rad51 diminished the ATPase activity³⁷. b The mutations of Rqt2 in the conserved residues in ATPase domain diminished RQC. c Rqt2-3 were distributed in heavy polysome fraction in Rqt2K316R mutant. d The expression levels of endogenously HA-tagged Rqt2, Rqt2-K316R, Rqt3, and Rqt4 proteins in Rqt2-K316R mutant cells

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