Abstract
BackgroundVanillin 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.ResultsIn 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.ConclusionsCells 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.
Highlights
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
Quantitative proteomic analysis reveals remarkable alterations in the protein abundance in response to vanillin To investigate the changes in protein abundance perturbed by vanillin stress, the proteomic differences were examined with the laboratory strain BY4741 cultivated with 5 mM vanillin for 15 h or without vanillin for 6 h when OD600 reached to 1.6
Here, the changes in general protein composition perturbed by vanillin stress and YRR1 deletion were investigated via quantitative proteome analysis
Summary
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. Lignocellulosic materials have been viewed as a major resources for bioethanol production worldwide because. The pretreatment of lignocellulose is inevitably generates many inhibitors, such as organic acids, furans, and phenolic compounds, which hamper microorganism growth and fermentation [4]. A guaiacyl phenol, has been considered as an important inhibitor of lignocellulosic hydrolysates, as it inhibits the viability of many microorganisms at very low concentration [5]. It is essential to understand the physiological mechanism of how vanillin inhibits S. cerevisiae growth and fermentation during the generation of vanillin-resistant S. cerevisiae cell factories to improve bioethanol and vanillin production
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