Abstract
Tremella fuciformis is a dimorphic fungus that can undertake a reversible transition between yeast-like conidia and hyphal forms. The transformation mechanism and proteomic differences between these two forms have not been reported. Therefore, in this study, we attempted to explore the differential protein profiles of dikaryotic yeast-like conidia from fruiting bodies and mycelia (FBMds) and dikaryotic mycelia (DM) by synthetically applying high-resolution MS1-based quantitative data-independent acquisition (HRMS1-DIA) full proteomics and parallel reaction monitoring (PRM) targeted proteomics. The results showed that a total of 5687 proteins were quantified, and 2220 of them (39.01%) showed more than a two-fold change in expression. The functional analysis of the differentially expressed proteins (DEPs) confirmed that the DEPs were mainly located in the membrane and nucleus. The FBMds tended to express proteins involved in biosynthesis, metabolism, DNA replication and transcription, and DNA damage repair. At the same time, DM exhibited an increased expression of proteins involved in signal transduction mechanisms such as the mitogen-activated protein kinase (MAPK) signaling pathway and the Ras signaling pathway. Further, phosphorylation analysis confirmed the importance of the MAPK signaling pathway in T. fuciformis dimorphism, and comparative metabolism analysis demonstrated the metabolic difference between FBMds and DM. The information obtained in the present study will provide new insights into the difference between FBMds and DM and lay a foundation for further research on the dimorphism formation mechanism of T. fuciformis.
Highlights
College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China; Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University, Abstract: Tremella fuciformis is a dimorphic fungus that can undertake a reversible transition between yeast-like conidia and hyphal forms
A while after the FBMds had been inoculated on the germination medium, hyphae germinated around the colonies, and this phenomenon is called the dimorphism of T. fuciformis (Figure 1A)
HRMS1-data-independent acquisition (DIA) and parallel reaction monitoring (PRM) were used to study the differential proteomics to understand the difference in protein expression between the two cell forms
Summary
College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China; Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University, Abstract: Tremella fuciformis is a dimorphic fungus that can undertake a reversible transition between yeast-like conidia and hyphal forms. In this study, we attempted to explore the differential protein profiles of dikaryotic yeast-like conidia from fruiting bodies and mycelia (FBMds) and dikaryotic mycelia (DM) by synthetically applying high-resolution MS1-based quantitative data-independent acquisition (HRMS1-DIA) full proteomics and parallel reaction monitoring (PRM). 1. Introduction with regard to jurisdictional claims in Tremella fuciformis is a typical dimorphic fungus with two cell types in its life history, the yeast-like conidia form and the hyphal form, and it transforms under the influence of the environment [1,2]. The dimorphism of T. fuciformis brings great difficulties to the breeding process, because it is very difficult to form mycelia [5] when basidiospores transform into yeast-like conidia. Previous studies showed that the nitrogen source, carbon source, carbon/nitrogen ratio, pH published maps and institutional affiliations
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
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.
