Ask about this productRelated genes to: PUS7 antibody
- Gene:
- PUS7 NIH gene
- Name:
- pseudouridine synthase 7
- Previous symbol:
- -
- Synonyms:
- FLJ20485
- Chromosome:
- 7q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-07
- Date modifiied:
- 2018-09-12
Related products to: PUS7 antibody
Related articles to: PUS7 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) is an abundant post-transcriptional modification found across all classes of RNA. It is widely speculated that Ψ inclusion in messenger RNAs (mRNAs) might provide an avenue for cells to control gene expression post-transcriptionally. Here we demonstrate that one of the principal mRNA pseudouridylating enzymes, pseudouridine synthase 7 (PUS7), exhibits a stress-induced accumulation in the cytoplasm of yeast and human epithelial lung cells. Stress-induced and cytoplasmic localization of PUS7 promotes Ψ-incorporation into hundreds of mRNA targets. In contrast, the modification status of tRNA sites targeted by PUS7 (Ψ13 and Ψ35) is unperturbed. Furthermore, engineered PUS7 cytoplasmic localization increases cellular fitness under reactive oxygen species (ROS) and divalent metal ion stress. Quantitative proteomics reveal a reshaping of the proteome upon PUS7 relocalization under stress. Collectively, our data demonstrate that PUS7 localization alters mRNA pseudouridylation patterns, reshapes the proteome, and influences cellular fitness. - Source: PubMed
Publication date: 2026/04/17
Ruan MinliEngels Sean MBurroughs Matthew RLi XiaoyanStower RosellaTzadikario TaliaPowell ConnorBloch DylanFanari OleksandraAkeson StuartEyler Daniel EWeidmann Chase ARouhanifard SaraJain MitenContreras Lydia MKoutmou Kristin S - Epitranscriptomic modifications are evolutionarily conserved changes to RNA and are present in all RNA types, including mRNA. Next to methylation, pseudouridine is also a prevalent modification found in mRNA and other RNA types. Pseudouridylation of RNA improves RNA stability, RNA stacking and translation fidelity. While mA RNA methylation has been demonstrated to regulate the activation of various immune cell types, such as T cells, dendritic cells or NK cells, insight into the role of pseudouridine in the immune system is limited. Trub1 is one of 13 pseudouridine synthases (PUS) and has been suggested to co-install the majority of pseudouridine residues on mRNA alongside the activity of PUS7 and has been reported to install pseudouridine in tRNA. Against this background, we hypothesized that Trub1 may regulate immune cell development, homeostasis or functional differentiation. Using conditional and global Trub1-deficient mice, in vivo competition in mixed bone marrow chimaeras and high-parametric flow cytometry, we interrogated the role of Trub1 in T cells, B cells, NK cells and myeloid cells. Despite our rigorous analyses and the identification of Trub1-dependent pseudouridine residues in mitochondrial tRNAs, we did not identify a significant role for Trub1-mediated pseudouridylation in immune cells at steady state or during disease. We hence reason that the role of Trub1 in mRNA pseudouridylation has previously been overestimated in computational studies or that co-installations of pseudouridine at other positions in the same RNA molecules may compensate for the lack of Trub1-installed modifications. - Source: PubMed
Publication date: 2026/03/24
Malviya VanshikaPham Cuong ThiMichiels LaurenSeldeslachts LauraMarchand VirginieVella GerlandaRangan LaurieMotorin YuriVande Velde GreetjeLemaitre PierreSchlenner Susan M - 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