The Response of Rhodotorula mucilaginosa to Patulin Based on Lysine Crotonylation

Abstract

Patulin (PAT) is a mycotoxin produced by some Penicillium, Aspergillus, and Byssochlamys species. Rhodotorula mucilaginosa is able to degrade PAT in vivo as well as in vitro, up till date, the process and molecular mechanism(s) involved patulin degradation still remains unknown. Protein lysine crotonylation (Kcr) plays an important role in regulating chromatin dynamics, gene expression, and metabolic pathways in mammals and eukaryotes. Investigation of the Kcr changes accompanying degradation of patulin in R. mucilaginosa were observed to investigate the mechanisms of patulin inhibition. Tandem mass tag (TMT) labeling and Kcro affinity enrichment, followed by high-resolution LC-MS/MS analysis, were used to perform quantitative lysine crotonylome analysis on R. mucilaginosa. Consequently, 1691 lysine crotonylation sites in 629 protein groups were identified, among which we quantified 1457 sites in 562 proteins. Among the quantified proteins, 79 and 46 crotonylated proteins were up-regulated and down-regulated, respectively. The differentially up expressed modified proteins were mainly involved in tricarboxylic acid cycle and gluconeogenic pathway. The differentially down expressed Kcr proteins were mainly classified to ribosome and carbohydrate transport and metabolism. Bioinformatic analyses were performed to annotate the quantifiable lysine crotonylated targets. Moreover, interaction networks and high confidence domain architectures of crotonylated proteins were investigated with the aid of bioinformatic tools, and these results showed that there was an increase in the number of yeasts with crotonylated proteins. The results also provided information on the various roles of crotonylation, which are involved in PAT degradation.

Functions and mechanisms of lysine crotonylation

“…In recent years, several landmark studies have revealed dramatically improved number of crotonylated lysine residues and crotonylated proteins (Table 1), and these proteins play roles in nearly all cellular processes including chromatin remodelling, metabolism, cell cycle and cellular organization. [13][14][15][16][17][18][19][20][21][22] Crotonylome mapping provides an important resource for discovering novel properties and regulatory functions of crotonylation.…”

First comprehensive proteomics analysis of lysine crotonylation in leaves of peanut (Arachis hypogaea L.)

“…Several recent reports have shown that crotonylation plays an important role in the regulation of various biological processes in humans, animals [19], plants [18,22] and microorganisms [21].…”

“…Global profiling of crotonylation has been reported in tobacco [18], zebrafish [19], rice [20], yeast [21], and papaya [22], which showed that crotonylation plays an important role in the regulation of various biological processes across kingdoms.…”

Recent trends in detecting, controlling, and detoxifying of patulin mycotoxin using biotechnology methods

“…Research on molecular mechanisms can ensure the sustainable development of biotechnology by serving as an inexhaustible source of information. Some current trends in the elucidation of mechanisms are presented: the mechanism of PAT degradation by yeast (Chen et al., 2017; Ianiri et al., 2013; Wang et al., 2019; Yang et al., 2018), mechanism of PAT biosynthesis (Li et al., 2019; Tannous et al., 2018), mechanism of PAT toxicity (Figure 1) (Ramalingam et al., 2019), the biocontrol mechanism (Zhang et al., 2018), mechanism of PAT adsorption by bacteria (Wang, Yue et al., 2015). There are confirmed biotechnological methods that are less used in PAT control.…”

“…Peptide networks can be useful in PAT control because post‐translational modifications (PTMs) are important in the cellular mechanism (Mauser & Jeltsch, 2019). For example, peptide arrays could be helpful in the study of PTMs during PAT degradation by R. mucilaginosa (Yang et al., 2018).…”