Ask about this productRelated genes to: PUS1 Blocking Peptide
- Gene:
- PUS1 NIH gene
- Name:
- pseudouridine synthase 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q24.33
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-06
- Date modifiied:
- 2018-09-12
Related products to: PUS1 Blocking Peptide
Related articles to: PUS1 Blocking Peptide
- Oral submucous fibrosis (OSF) is a chronic, potentially malignant disorder strongly associated with areca nut chewing. Cuproptosis, a newly identified form of cell death, may play a role in OSF progression, but the mechanisms remain unclear. This study aimed to explore the involvement of cuproptosis in OSF. Here, we observed a significant increase in cuproptosis markers (FDX1 and LIAS) in OSF lesion tissues compared to normal oral mucosa. In vitro, arecoline induced cuproptosis predominantly in epithelial cells, characterized by increased FDX1 and LIAS expression, disrupted lipoylation of DLAT, and elevated intracellular Cu²⁺ accumulation. An epigenetic modification PCR array revealed that arecoline most markedly upregulated PUS1, a pseudouridine (Ψ) modification synthase. Functional knockdown of PUS1 alleviated arecoline-induced cuproptosis, as evidenced by reduced Cu²⁺ levels and restored lipoic acid expression. Dot blot and PA-ψ-seq further demonstrated that arecoline-induced PUS1 upregulation altered the global tRNA pseudouridylation landscape, with enrichment of Ψ peaks in Wnt- and copper transport-related transcripts. PUS1 knockdown markedly attenuated arecoline-induced β-catenin nuclear localization and the upregulation of MYC, FZD6, CTNNB1, NFAT5, SLC25A39, and VDAC2. In conclusion, we reveal a previously unrecognized mechanism whereby arecoline promotes OSF via PUS1-dependent pseudouridylation remodeling and epithelial cuproptosis, offering novel therapeutic targets for OSF intervention. - Source: PubMed
Publication date: 2026/07/27
Lin ShigengDeng WeiWen QitaoXu Xiongjun - Assembly of the mitochondrial ribosome (mitoribosome) is a crucial step in mitochondrial gene expression. This process facilitates mitochondrial translation, which produces essential subunits of the oxidative phosphorylation machinery-the cell's primary energy-producing machinery. Disruptions in mitoribosome assembly can lead to severe human diseases. Given its fundamental importance, detailed structural analysis of mitoribosome assembly pathways is essential for advancing our understanding of mitochondrial function in both health and disease. In this study, we characterize twelve distinct assembly states of the mitoribosomal small subunit (mtSSU) isolated from human cells. Our findings reveal the intricate details of the final maturation stages of the mtSSU platform, decoding center, and the 3'-end of 12S rRNA. This process is governed by coordinated actions of assembly factors that ensure precise, stepwise rRNA folding and the integration of mitoribosomal proteins into the developing subunit. Our approach identifies pseudouridine synthase PUS1 and initiation factor mtIF2 as assembly factors, expanding their known roles beyond mt-tRNA maturation and translation, respectively. In addition, the identified assembly intermediates provide insight into the modular nature of mtSSU biogenesis in mitochondria and further link late-stage assembly to the acquisition of translational competence. - Source: PubMed
Publication date: 2026/06/24
Singh VivekShiriaev DmitriiBilalli LorinaKhawaja AnasRorbach Joanna - Hepatocellular carcinoma (HCC) is a genomically heterogeneous malignancy with substantial variability in prognosis and therapeutic response. Pseudouridine () modification is an evolutionarily conserved RNA modification involved in RNA structure stabilization and translational regulation; however, the genomic and functional relevance of pseudouridine modification-related genes (PDGs) in HCC remains poorly defined. - Source: PubMed
Publication date: 2026/06/22
Gan ZeyingFan TingyuanWang WenjuanQiao XiaoZhao Mingming - BACKGROUND: Studies have shown that mitochondrial dysfunction in macrophages worsens inflammation and impedes repair after acute myocardial infarction (AMI). This study aimed to identify and validate biomarkers of AMI associated with mitochondria-related genes (MRGs) and macrophage polarization-related genes (MPRGs), offering new targets and strategies for therapeutic intervention of AMI. METHODS: In this study, the GSE61144 and GSE60993 datasets were employed. Initially, candidate genes were identified by overlapping the differentially expressed genes (DEGs) from differential expression analysis, key module genes from weighted gene co-expression network analysis (WGCNA), and MRGs. Then, biomarkers were identified by machine learing, receiver operating characteristic (ROC), and gene expression analyses. Finally, functional enrichment, immune infiltration, drug prediction, and reverse transcription quantitative polymerase chain reaction (RT-qPCR) analyses were performed to explore the roles of these biomarkers. RESULTS: The study identified APEX1, ECHDC2, NME3, and PUS1 as biomarkers associated with AMI, all of which exhibited reduced expression in AMI samples. RT-qPCR results further validated these findings. Notably, all 4 biomarkers were predominantly co-enriched in the “ribosome” pathway, highlighting its significance in AMI. Additionally, 11 differential immune cells were identified. Correlation analysis revealed that these biomarkers showed the strongest positive correlations with activated CD8 T cells and the most negative correlations with neutrophils. Drug prediction indicated that valproic acid, which targeted all 4 biomarkers, could be a promising therapeutic option for AMI. CONCLUSIONS: In this study, APEX1, ECHDC2, NME3, and PUS1 were identified as biomarkers for AMI, with their expression levels validated in clinical samples. These findings offered a potential theoretical foundation for developing targeted treatments for AMI. CLINICAL TRIAL NUMBER: Not applicable. - Source: PubMed
Publication date: 2026/05/29
Qu NanBai FawenLan Jin - Pseudouridine is the most abundant RNA base modification due to its prevalence in tRNA and rRNA, where it serves as a key modulator of structure and function. Yet even in a widely used model organism, the budding yeast , the positions of all pseudouridines in tRNA have not been completely annotated. Using Nanopore direct RNA sequencing (DRS), an established method for detecting RNA pseudouridylation positions, we sequenced cytosolic tRNA from eight pseudouridine synthase (PUS) knockout strains, including deletion strains of Pus1, Pus3, and Pus7. Analysis of these data verified thirty-four existing pseudouridine annotations and predicted eleven previously unannotated pseudouridine sites. Our analysis revealed DRS signal changes at several non-uridine sites with the loss of a PUS, including apparent changes in modification abundances at position 37 upon deletion of Pus3. LC-MS/MS and primer extension assays, however, indicated no change in the abundance of these modifications with the loss of Pus3. Our analysis underscores the need for caution in interpreting DRS-based signal changes, particularly in modification-dense regions. Combining existing modification annotations for the thirty-one isoacceptors in the Modomics database with our dataset that added annotations for the remaining eleven isoacceptors, we created a map of all detected pseudouridines, and the enzymes responsible for their catalysis, across the forty-two cytosolic tRNA isoacceptors. - Source: PubMed
Publication date: 2026/05/01
Barry Margaret LAbu-Shumays Robin LBarnes Lauren EShaw Ethan AReinsch Julia LVaaler Abigail LBasham Zachary DJain MitenKoutmou Kristin SGarcia David M