Abstract
Thermophilic fungi are eukaryotic species that grow at high temperatures, but little is known about the underlying basis of thermophily at cell and molecular levels. Here the proteome and N-glycoproteome of Chaetomium thermophilum at varying culture temperatures (30, 50, and 55°C) were studied using hydrophilic interaction liquid chromatography enrichment and high-resolution liquid chromatography–tandem mass spectroscopy analysis. With respect to the proteome, the numbers of differentially expressed proteins were 1,274, 1,374, and 1,063 in T50/T30, T55/T30, and T55/T50, respectively. The upregulated proteins were involved in biological processes, such as protein folding and carbohydrate metabolism. Most downregulated proteins were involved in molecular functions, including structural constituents of the ribosome and other protein complexes. For the N-glycoproteome, the numbers of differentially expressed N-glycoproteins were 160, 176, and 128 in T50/T30, T55/T30, and T55/T50, respectively. The differential glycoproteins were mainly involved in various types of N-glycan biosynthesis, mRNA surveillance pathway, and protein processing in the endoplasmic reticulum. These results indicated that an efficient protein homeostasis pathway plays an essential role in the thermophily of C. thermophilum, and N-glycosylation is involved by affecting related proteins. This is the novel study to reveal thermophilic fungi’s physiological response to high-temperature adaptation using omics analysis, facilitating the exploration of the thermophily mechanism of thermophilic fungi.
Highlights
Glycosylation, the attachment of glycans to proteins, is a posttranslational modification to produce significant structural changes to proteins (Ge et al, 2018)
A great many differentially expressed proteins and N-glycoproteins of C. thermophilum grown at 30, 50, and 55◦C were identified by proteomics and glycomics analysis. These results indicate that protein homeostasis pathways play a key role in the thermophily of C. thermophilum
The proteome and N-glycoproteome of C. thermophilum in response to high temperatures were analyzed by the combination of hydrophilic interaction liquid chromatography (HILIC)-based enrichment and high-resolution liquid chromatography–tandem mass spectroscopy (LC-MS/MS) analyses for the first time
Summary
Glycosylation, the attachment of glycans to proteins, is a posttranslational modification to produce significant structural changes to proteins (Ge et al, 2018). Glycosylation is considered the most complicated posttranslational modification due to the multiple enzymatic steps (Eichler, 2020). Glycans are encoded in a complex dynamic network containing hundreds of genes, which form the enzymes for glycan synthesis. Molecular events, such as transferring sugars from one substrate to another, linking monosaccharides, and trimming sugars from glycan structures, are involved in glycosylation. N-linked glycans are derived from a core 14-sugar unit assembled in the cytoplasm and endoplasmic reticulum in eukaryotes. N-linked glycan’s core structure comprises 14 residues (three glucose residues, nine mannose residues, and two N-acetyl glucosamine residues) (Munro, 2009)
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