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. 2018 Aug 9;8:11904. doi: 10.1038/s41598-018-30383-z

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© The Author(s) 2018

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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2D proteome analysis of rrp8 mutant. (A) Scanned images of a typical 2-D DIGE gel of 50 µg protein from the Cy3 labeled protein pool used for the rrp8 mutant strain (left gel: pH 4–7, right gel: pH 6–11). Differentially expressed proteins are annotated and were identified using ESI-MS/MS. Differentially expressed protein spots are annotated in red (down-regulated) or green (up-regulated). (B) DeCyder output showing the representative differentially expressed protein spots of Asc1, Eno2, Pgk1, Rps5, Sol3 and Rps10A along with their 3-D fluorescence intensity profiles. (C and D) Sol3 up-regulation is related to loss of m¹A₆₄₅ methylation. Western blot analysis using anti-HA antibodies to analyze the expression of 6xHA tagged SOL3 in wild-type, Δrrp8 and rrp8^G209R mutant cells. As loading control, PYK1 was detected with a specific antibody. The represented fold changes in SOL3 expression were quantified using ImageJ software (http://imagej.nih.gov/ij/).