Abstract
Redox modification, a post-translational modification, has been demonstrated to be significant for many physiological pathways and biological processes in both eukaryotes and prokaryotes. However, little is known about the global profile of protein redox modification in fungi. To explore the roles of redox modification in the plant pathogenic fungi, a global thiol proteome survey was performed in the model fungal pathogen Magnaporthe oryzae. A total of 3713 redox modification sites from 1899 proteins were identified through a mix sample containing mycelia with or without oxidative stress, conidia, appressoria, and invasive hyphae of M. oryzae. The identified thiol-modified proteins were performed with protein domain, subcellular localization, functional classification, metabolic pathways, and protein–protein interaction network analyses, indicating that redox modification is associated with a wide range of biological and cellular functions. These results suggested that redox modification plays important roles in fungal growth, conidium formation, appressorium formation, as well as invasive growth. Interestingly, a large number of pathogenesis-related proteins were redox modification targets, suggesting the significant roles of redox modification in pathogenicity of M. oryzae. This work provides a global insight into the redox proteome of the pathogenic fungi, which built a groundwork and valuable resource for future studies of redox modification in fungi.
Highlights
Protein features and functions are modulated by sequence of the amino acids and by post-translational modifications (PTMs), such as acetylation, lipidation, methylation, and oxidation–reduction modification
In order to identify as many redox peptides as possible, we gathered samples from mycelia, conidia, appressorium, infection hyphae of M. oryzae, as well as mycelia shocked with reactive oxygen species
3713 redox sites belonging to 1899 proteins have been identified, while 2859 redox sites from 1551 proteins were identified by both two repeats, as shown in Figure 1B and Supplementary Table 1
Summary
Protein features and functions are modulated by sequence of the amino acids and by post-translational modifications (PTMs), such as acetylation, lipidation, methylation, and oxidation–reduction modification (as known as redox modification). In PTMs, the redox modification on cysteine residues is an important source of regulations on protein functions (Go and Jones, 2013; Sievers et al, 2018), which impacts many physiological pathways and biological processes (Zhao and Jensen, 2009; Baraibar and Friguet, 2013; Olsen and Mann, 2013). The reactive thiol groups attached to cysteine residues are responsible to the redox modifications by shifting from reduction to oxidation or (Winterbourn and Hampton, 2008; Hancock, 2009; Paulsen and Carroll, 2010), where the shifting is either irreversible (e.g., sulfonic acid) or reversible (e.g., disulfide bonds) (Murray and Van Eyk, 2012). The consequence of redox modification on proteins varies depending on both protein itself (e.g., biochemical properties and three-dimensional arrangement) and reactive oxygen species (ROS) (e.g., abundance and species) (Corcoran and Cotter, 2013), which introduces complexes and uncertainties to redox proteome
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
