Ask about this productRelated genes to: PUS1 antibody
- 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 antibody
Related articles to: PUS1 antibody
- 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 - Pseudouridine (Ψ) modification is a prevalent epitranscriptomic mark with critical roles in carcinogenesis; however, the function of its catalytic "writer" enzyme, pseudouridine synthase 1 (PUS1), in renal cell carcinoma (RCC) remains elusive. Our analysis revealed that mRNA is upregulated in RCC and is associated with an unfavorable prognosis. Strikingly, this transcriptional upregulation results in a concomitant and exclusive increase in the protein abundance of PUS1 isoform 2. Mechanistically, although PUS1 markedly enhances global mRNA translation, this effect is not directly mediated via Ψ modification of either mRNA or tRNA. Instead, PUS1 regulates pre-mRNA splicing, and its deficiency induces elevated intron retention. This, in turn, culminates in the formation of double-stranded RNA (dsRNA), which subsequently activates the innate antiviral immune response and inhibits global translation. Furthermore, depletion of PUS1 in tumor cells significantly sensitizes RCC to immune checkpoint blockade therapy. Collectively, our findings demonstrate that PUS1 shields tumor cells from endogenous dsRNA accumulation and the consequent detrimental innate immune activation, thereby unveiling a novel and promising therapeutic strategy for RCC. - Source: PubMed
Publication date: 2026/03/25
Zhu ZiweiLu ZeyiLi FanXu ZhehaoWang RuyueLi YangLu HaohuaDing YimingLuo WenqinLin YudongLu YiMao XudongLi MengxuanWang ZiyuanDing LifengXia LiqunLi Gonghui - Transfer RNA-derived fragments (tRFs) are a recently discovered class of short noncoding RNAs widely distributed in various tissues and cell types. They are involved in the regulation of gene expression and play important roles in both physiological and pathological processes, garnering growing attention. However, the functions and underlying mechanisms of most tRFs in tumorigenesis and progression remain largely unclear. Through small RNA sequencing of nasopharyngeal carcinoma (NPC) and adjacent tissues, we found that among the top 30 highly expressed tRFs in NPC tissues, 13 were derived from lysine tRNAs, forming the 5′-tRF-Lys cluster. This cluster was found to promote NPC cell proliferation, invasion, and migration. Mechanistically, 5′-tRF-Lys binds to the 3′-untranslated region (3′-UTR) of messenger RNA (mRNA), suppressing its expression and thereby activating the Hippo/YAP signaling pathway to drive tumor progression. The elevated expression of pseudouridine synthases and in NPC tissues catalyzes pseudouridine modification of tRNA-Lys, facilitating its cleavage into 5′-tRF-Lys and accounting for its upregulation. Notably, the -targeting small-molecule inhibitor mogroside IV-e effectively reversed malignant phenotypes in both in vitro and in vivo NPC models. This study uncovers a novel mechanism in which pseudouridine synthases and drive the biogenesis of the tRF-Lys cluster, promoting NPC malignancy by suppressing and activating the Hippo/YAP signaling pathway. These findings highlight the therapeutic potential of targeting pseudouridine synthases to reduce tRF-Lys production as a novel strategy for NPC treatment. - Source: PubMed
Publication date: 2026/02/28
Ren DaixiYang MeiMo YongzhenYan QijiaShi LeiZhang ShanshanGong ZhaojianGuo CanZhou MingXiang BoTan MingLi GuiyuanChen PanXiong WeiZeng Zhaoyang - 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 - RNA modification enzymes (RMEs) are key post-transcriptional regulators that impact RNA stability, translation, and splicing. Dysregulation of RMEs is closely associated with tumor initiation and progression. However, their global regulatory patterns and clinical relevance across cancer types remain incompletely characterized. - Source: PubMed
Publication date: 2026/01/28
Zhan QianqianSun HuihuiWang XiangtingLiang Xiaolin