Project description:Stropharia rugosoannulata (S. rugosoannulata) is a fungus with great edible and nutritional values; however, the development mechanism of its fruiting body has not been studied. Thus, this study aimed to analyze the differentially expressed genes (DEGs) in four stages; primordia stage (Sra1), young mushroom stage (Sra2), picking stage (Sra3), and opening umbrella stage (Sra4). Therefore, total RNA was extracted for further RNA-sequencing analysis. In three pairwise comparison groups (PCGs), Sra1 vs. Sra2, Sra2 vs. Sra3, and Sra3 vs. Sra4, a total of 3,112 DEGs were identified among the three PCGs. A GO analysis of the DEGs showed that there were 21 terms significantly enriched in Sra1 vs. Sra2 PCG. There was no significantly enriched GO term in the other two PCGs. Furthermore, KEGG pathway analysis showed that these DEGs were mainly enriched in glucose and amino acid metabolisms. Moreover we found that intron retention (IR) and the alternative 3′ splice site (A3SS) accounted for more than 80%. The development of the S. rugosoannulata fruiting body mainly involved glucose and amino acid metabolisms. IR and A3SS were the two main types of ASE, which played an important role in the development and maturation of the S. rugosoannulata fruiting body.
| S-EPMC9318406 | biostudies-literature
Project description:Transcriptome analysis of Stropharia rugosoannulata fruiting body
Project description:To reveal the structural characteristics and angiotensin-converting enzyme (ACE) inhibition mechanism of Stropharia rugosoannulata mushroom peptides prepared by multifrequency ultrasound, the peptide distribution, amino acid sequence composition characteristics, formation pathway, and ACE inhibition mechanism of S. rugosoannulata mushroom peptides were studied. It was found that the peptides in S. rugosoannulata mushroom samples treated by multifrequency ultrasound (probe ultrasound and bath ultrasound mode) were mainly octapeptides, nonapeptides, and decapeptides. Hydrophobic amino acids were the primary amino acids in the peptides prepared by ultrasound, and the amino acid dissociation of the peptide bonds at the C-terminal under the action of ultrasound was performed mainly to produce hydrophobic amino acids. Pro and Val (PV), Arg and Pro (RP), Pro and Leu (PL), and Asp (D) combined with hydrophobic amino acids were the characteristic amino acid sequence basis of the active peptides of the S. rugosoannulata mushroom. The docking results of active peptides and ACE showed that hydrogen bond interaction remained the primary mode of interaction between ACE and peptides prepared by ultrasound. The peptides can bind to the amino acid residues in the ACE active pocket, zinc ions, or key amino acids in the domain, and this results in inhibition of ACE activity. Cation-pi interactions also played an important role in the binding of mushroom peptides to ACE. This study explains the structural characteristics and ACE inhibition mechanism used by S. rugosoannulata mushroom peptides prepared by ultrasound, and it will provide a reference for the development and application of S. rugosoannulata mushroom peptides.
