Crosstalk between proteins expression and lysine acetylation in response to patulin stress in Rhodotorula mucilaginosa

Xiangfeng Zheng,Maurice Tibiru Apaliya,Hongyin Zhang,Xiaoyun Zhang,Lina Zhao,Qiya Yang

doi:10.1038/s41598-017-14078-5

Xiangfeng Zheng, Maurice Tibiru Apaliya + Show 4 more

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https://doi.org/10.1038/s41598-017-14078-5

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Journal: Scientific Reports	Publication Date: Oct 18, 2017
Citations: 18	License type: open-access

Affiliation: Jiangsu University

Abstract

The proteomic and lysine acetylation (Kac) changes, accompanying degradation of patulin in Rhodotorula mucilaginosa were analyzed using tandem mass tagging and N6-acetyllysine affinity enrichment followed by LC-MS/MS. Proteomic results showed that expression level of short-chain reductase protein and glutathione S-transferase involved in detoxification was significantly up-regulated. In addition, the expression levels of zinc-binding oxidoreductase and quinone oxidoreductase that are involved in antioxidant process, ABC transport and MFS transport responsible for chemical transport were activated when treated with patulin. The quantitative real time PCR (qRT-PCR) result also indicated these genes expression levels were increased when treated with patulin. Kac changes accompanying degradation of patulin in R. mucilaginosa were also observed. Totally, 130 Kac sites in 103 proteins were differentially expressed under patulin stress. The differentially up expressed modified proteins were mainly involved in tricarboxylic acid cycle and nuclear acid biosynthesis. The differentially down expressed Kac proteins were mainly classified to ribosome, oxidative phosphorylation, protein synthesis and defense to stress process. Our results suggest that patulin exposure prompt R. mucilaginosa to produce a series of actions to resist or degrade patulin, including Kac. In addition, the Kac information in R. mucilaginosa and Kac in response to patulin stress was firstly revealed.

Highlights

The proteomic and lysine acetylation (Kac) changes, accompanying degradation of patulin in Rhodotorula mucilaginosa were analyzed using tandem mass tagging and N6-acetyllysine affinity enrichment followed by LC-MS/MS
Among the differentially down-regulated proteins (DDPs), Ribonucleoside-diphosphate reductase (RNR) which is involved in nuclear acid biosynthesis[40] and some proteins which are involved in amino acid metabolism were DDP (Supplementary Table S3)
The expression level of zinc-binding oxidoreductase (ZOD), NAD dependent oxidoreductase, quinone oxidoreductase and cytochrome-c peroxidase which are involved in oxidation-reduction process, ABC and MFS which were involved in transport processes were differentially up-regulated (DUR) both at gene and protein level

Summary

Introduction

The proteomic and lysine acetylation (Kac) changes, accompanying degradation of patulin in Rhodotorula mucilaginosa were analyzed using tandem mass tagging and N6-acetyllysine affinity enrichment followed by LC-MS/MS. The expression levels of zinc-binding oxidoreductase and quinone oxidoreductase that are involved in antioxidant process, ABC transport and MFS transport responsible for chemical transport were activated when treated with patulin. 130 Kac sites in 103 proteins were differentially expressed under patulin stress. Many yeasts Rhodosporidium kratochvilovae[13], Pichia caribbica[14,15] and Rhodosporidium paludigenum[16] have been proved to degrade patulin through enzymes catalytic process. P. caribbica and R. paludigenum were shown to degrade patulin by the production of intracellular enzymes[15,16]. The degradation products of patulin using antagonistic yeast have been identified, but the process and molecular mechanism(s) involved still remains unknown. Patulin was reported to induce the accumulation of ROS23. The results indicated that patulin induced yeast gene expression profiles similar to gene expression patterns obtained after treatment with synthetic chemicals[25]

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