Ask about this productRelated genes to: RPUSD2 Blocking Peptide
- Gene:
- RPUSD2 NIH gene
- Name:
- RNA pseudouridine synthase domain containing 2
- Previous symbol:
- C15orf19
- Synonyms:
- C18B11, FLJ31409, PUS9
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-02
- Date modifiied:
- 2018-09-12
Related products to: RPUSD2 Blocking Peptide
Related articles to: RPUSD2 Blocking Peptide
- Pseudouridine (Ψ) is an abundant modification in small RNA catalyzed by multiple pseudouridine synthases (PUSs). However, the substrate specificity of human PUSs remains elusive. Here, we adopted PRAISE, a quantitative Ψ detection method, to profile pseudouridylation in small RNA, including cytosolic and mitochondrial tRNAs, snRNA, and snoRNA. We found that snoRNA pseudouridylation is mediated not only by RNA-guided DKC1, but also by the stand-alone enzyme PUS7 at a specific site. Interestingly, several PUS enzymes, including PUS1, RPUSD1, and PUS7, which install nearby Ψ sites within tRNA anticodon stem-loop, can influence pseudouridylation catalyzed by other PUSs, revealing an unrecognized interplay during Ψ formation. For the three RluA family enzymes, RPUSD1 catalyzes the canonical Ψ30 in tRNA-Ile and Ψ72 in tRNA-Arg isoacceptors. RPUSD2 pseudouridylates Ψ31 of mt-tRNA, Ψ32 of mt-tRNA and mt-tRNA, whereas RPUSD3 lacks tRNA activity. Together, our quantitative Ψ profiling characterized PUS tRNA substrates and revealed unexpected PUS interplay. - Source: PubMed
Publication date: 2026/02/16
Liu WenqingMa YichenWang LipingLu BoDong YuyangZhuang YuanHe BoZhang MeilingYi Chengqi - Nephrolithiasis is a highly prevalent urological condition with a marked recurrence tendency. However, the molecular mechanisms within the local renal tissue microenvironment remain unclear—largely due to the limited availability of relevant clinical specimens, which has hindered in-depth research efforts. In this study, we conducted label-free quantitative proteomics on paired stone-containing (S) and non-stone (NS) renal papillary tissues. All these samples were obtained from 6 patients with calcium oxalate stones. To reliably identify differentially expressed proteins (DEPs), we employed two statistical models simultaneously: unpaired analysis (fold change |FC| ≥ 1.2, p < 0.05) and patient-specific paired analysis (|FC| ≥ 1.5, p < 0.05). Group-wise comparison identified a total of 41 DEPs. Subsequent pathway analysis showed that these DEPs were associated with several key biological processes, including extracellular matrix interaction, oxidative phosphorylation, and glycosaminoglycan metabolism. Notably, paired analysis across individuals revealed a shared core of dysregulated proteins. Interestingly, LPCAT3 exhibited altered expression in all 6 patients; in contrast, RPUSD2, SLC34A3, UCK1, ERVK-19, and ACSL5 were dysregulated in 5 patients. This recurrent signature suggests the existence of convergent pathological mechanisms, roughly involving dysregulated lipid metabolism (LPCAT3, ACSL5), disrupted phosphate homeostasis (SLC34A3), abnormal nucleotide metabolism (UCK1), mitochondrial dysfunction (RPUSD2), and inflammatory responses (ERVK-19). Our study delineates the proteomic landscape of the stone-containing renal microenvironment in humans and uncovers a robust, patient-shared molecular signature. These recurrent core proteins—particularly LPCAT3—hold promise as novel therapeutic targets for preventing stone recurrence by targeting underlying local pathological processes, which offers new insights and directions for clinical intervention. - Source: PubMed
Publication date: 2026/02/12
Jia YiyingShu MengZhang ShuweiChen MinjieFang ZiyuGao Xiaofeng - Pseudouridine (Ψ) is one of the most abundant RNA modifications in human cells, introduced post-transcriptionally by pseudouridine synthases (PUS). Despite its prevalence, the biological functions of Ψ remain poorly understood, largely due to the limited knowledge linking specific PUS enzymes to their targets. Here, to address this gap, we systematically knocked out or knocked down nine stand-alone PUS in HCT116 cells and mapped their Ψ profiles using 2-bromoacrylamide-assisted cyclization sequencing. Through this approach, we uncovered previously unknown targets of several PUS enzymes, including RPUSD1, RPUSD2, PUS3, PUSL1 and PUS7L. In addition, we revealed that TRUB1 and PUS10 function redundantly to catalyse the highly conserved Ψ55 modification in cytosolic tRNAs. Intriguingly, we found that RPUSD3 and TRUB2 do not exhibit noticeable enzymatic activities in human cells. By integrating these findings with earlier results for TRUB1, PUS7 and PUS1, we constructed a comprehensive map of stand-alone PUS-dependent Ψ modifications across human tRNAs. Using this map, we further demonstrated that different PUS enzymes introduce Ψ modifications at distinct stages of pre-tRNA processing. - Source: PubMed
Publication date: 2025/10/24
Xu HaiqiKong LinzhenLi MengjiePisignano GiuseppinaCheng JingfeiFeng FengMehdipour ParinazSong Chun-Xiao - Epitranscriptomic modifications regulate gene expression and have been implicated in cancer, including breast cancer. Using the SCAN-B cohort, we analyzed 49 messenger RNA modification regulators (mRMPs) across breast cancer subtypes. In the basal subtype, we found significant overexpression of mA readers (IGF2BP1-3), mC regulators (NSUN5, ALYREF, YBX1, YBX2), pseudouridine [PUS1, MARS (or MetRS), RPUSD2], and RNA editing enzymes [APOBEC3A (A3A), A3G, ADAR1], all linked to poor survival. Conversely, the mA writer METTL14 was downregulated. Our findings highlight key mRMPs as potential biomarkers and therapeutic targets, underscoring the role of RNA modifications in breast cancer progression. - Source: PubMed
Publication date: 2025/09/03
Peula CarlosEsteva-Socias MargalidaKumari KanchanDassi ErikAguilo Francesca - The pseudouridine synthases (PUSs) have been reported to be associated with cancers. However, their involvement in hepatocellular carcinoma (HCC) has not been well documented. Here, we assess the roles of PUSs in HCC. RNA sequencing data of TCGA-LIHC and LIRI-JP were downloaded from the Cancer Genome Atlas (TCGA) and the International Cancer Genome Consortium (ICGC), respectively. GSE36376 gene expression microarray was downloaded from the Gene Expression Omnibus (GEO). Proteomics data for an HBV-related HCC cohort was obtained from the CPTAC Data Portal. The RT-qPCR assay was performed to measure the relative mRNA expression of genes in clinical tissues and cell lines. Diagnostic efficiency was evaluated by the ROC curve. Prognostic value was assessed using the Kaplan-Meier curve, Cox regression model, and time-dependent ROC curve. Copy number variation (CNV) was analyzed using the GSCA database. Functional analysis was carried out with GSEA, GSVA, and clusterProfiler package. The tumor microenvironment (TME) related analysis was performed using ssGSEA and the ESTIMATE algorithm. We identified 7 that were significantly upregulated in HCC, and 5 of them (, , , , and ) were independent risk factors for patients' OS. Meanwhile, the protein expression of DKC1, PUS1, and PUS7 was also upregulated and related to poor survival. Both mRNA and protein of these PUSs were highly diagnostic of HCC. Moreover, the CNV of , , , and was also associated with prognosis. Further functional analysis revealed that PUSs were mainly involved in pathways such as genetic information processing, substance metabolism, cell cycle, and immune regulation. PUSs may play crucial roles in HCC and could be used as potential biomarkers for the diagnosis and prognosis of patients. - Source: PubMed
Publication date: 2022/11/10
Jin ZhipengSong MengyingWang JianpingZhu WenjingSun DongxuLiu HuayuanShi Guangjun