Journal
MICROBIAL CELL FACTORIES
Volume 20, Issue 1, Pages -Publisher
BMC
DOI: 10.1186/s12934-021-01633-z
Keywords
YRR1; Quantitative proteomics; Vanillin resistance; Bioethanol; Saccharomyces cerevisiae
Categories
Funding
- National Key R&D Program of China [2018YFB1501401]
- National Natural Science Foundation of China [31870063]
- Shandong Provincial Natural Science Foundation [ZR2019BC080]
- Key R&D Project of Shandong Province [2019JZZY010906]
- Major Program of Shandong Province Natural Science Foundation [ZR2018ZB0209]
- Special Funds for International Cooperative Research of Qilu University of Technology (Shandong Academy of Sciences) [QLUT-GJHZ2018009]
- State Key Laboratory of Biobased Material and Green Papermaking, Qilu University of Technology, Shandong Academy of Sciences [ZZ20190306]
- ESI Cultivation discipline of Biology and Biochemistry, Qilu University of Technology [202015]
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Vanillin is an important phenolic inhibitor in Saccharomyces cerevisiae, inhibiting the translation process. Deletion of YRR1 enhances vanillin resistance by promoting translation-related processes. Proteomic changes induced by vanillin stress and YRR1 deletion provide insights into yeast's protective response to vanillin.
Background Vanillin is one of the important phenolic inhibitors in Saccharomyces cerevisiae for bioconversion of lignocellulosic materials and has been reported to inhibit the translation process in cells. In our previous studies, it was confirmed that the deletion of the transcription factor gene YRR1 enhanced vanillin resistance by promoting some translation-related processes at the transcription level. In this work, we investigated the effects of proteomic changes upon induction of vanillin stress and deletion of YRR1 to provide unique perspectives from a transcriptome analysis for comprehending the mechanisms of YRR1 deletion in the protective response of yeast to vanillin. Results In wild-type cells, vanillin reduced two dozens of ribosomal proteins contents while upregulated proteins involved in glycolysis, oxidative phosphorylation, and the pentose phosphate pathway in cells. The ratios of NADPH/NADP(+) and NADH/NAD(+) were increased when cells responded to vanillin stress. The differentially expressed proteins perturbed by YRR1 deletion were much more abundant than and showed no overlaps with transcriptome changes, indicating that Yrr1 affects the synthesis of certain proteins. Forty-eight of 112 upregulated proteins were involved in the stress response, translational and transcriptional regulation. YRR1 deletion increased the expression of HAA1-encoding transcriptional activator, TMA17-encoding proteasome assembly chaperone and MBF1-encoding coactivator at the protein level, as confirmed by ELISA. Cultivation data showed that the overexpression of HAA1 and TMA17 enhanced resistance to vanillin in S. cerevisiae. Conclusions Cells conserve energy by decreasing the content of ribosomal proteins, producing more energy and NAD(P)H for survival in response to vanillin stress. Yrr1 improved vanillin resistance by increasing the protein quantities of Haa1, Tma17 and Mbf1. These results showed the response of S. cerevisiae to vanillin and how YRR1 deletion increases vanillin resistance at the protein level. These findings may advance our knowledge of how YRR1 deletion protects yeast from vanillin stress and offer novel targets for genetic engineering of designing inhibitor-resistant ethanologenic yeast strains.
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