Ask about this productRelated genes to: TUT1 antibody
- Gene:
- TUT1 NIH gene
- Name:
- terminal uridylyl transferase 1, U6 snRNA-specific
- Previous symbol:
- RBM21
- Synonyms:
- FLJ22347, FLJ22267, FLJ21850, PAPD2, TUTase, TENT1
- Chromosome:
- 11q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-07
- Date modifiied:
- 2018-04-20
Related products to: TUT1 antibody
Related articles to: TUT1 antibody
- Numerous studies have identified a large number of miRNA editing sites via deep sRNA sequencing profiling of tissue samples. However, the single-cell landscape of miRNA editing patterns has remained largely unknown to date. To investigate miRNA editing and mutation characteristics at single cell level, this study analyzed miRNA editing and mutation events in 448 single-cell small RNA sequencing profiles from 5 different cell types. Our results revealed that PCA and clustering analysis, performed based on the editing levels of identified miRNA editing sites, could distinguish distinct cell types, indicating that miRNA editing patterns are cell-type-specific across different cellular populations. We further demonstrated that a subset of miRNA editing sites exhibited strict cell-type-specific editing patterns. Meanwhile, within the same cell type, the identified sites presented different distributions of editing levels in different cells. A fraction of sites showed highly variable editing levels among different cells of the same cell type, while some sites displayed relatively uniform and consistent editing patterns. An A-to-I editing site in hsa-mir-376c, i.e., hsa-mir-376c 48 A g, showed a significantly higher editing level in glioblastoma cells than in naive embryonic stem cells, suggesting a potential role in the initiation and progression of glioblastoma. Furthermore, our results also suggest that in leukemia cells, TENT4A, TENT5A, TENT5B, TENT5C, TENT5D, and TUT1 may mediate the non-templated nucleotide additions to the 3'ends of miRNAs. - Source: PubMed
Publication date: 2026/04/09
Mao ChunyiGuo HaoXie WenpingXu YueZhang HongjiaLuo KangYang JunZheng Yun - Post-transcriptional maturation of the U6 snRNA 3'-end, important for spliceosome assembly, is catalyzed by sequential actions of TUT1 and USB1. It is believed that the TUT1-catalyzed oligo(U) tail at the U6 snRNA 3'-end serves merely as a substrate for USB1 to generate a final 2',3'-cyclic phosphate group to mature the U6 snRNA. However, biallelic inactivation of TUT1 or USB1 is linked to distinct human developmental disorders, suggesting that they have different physiological functions. Here, using genetically engineered mouse models, we show that Tut1 is required to maintain stem cell pools during embryogenesis, whereas unexpectedly Usb1 is dispensable for this. Loss of Tut1 weakens the interaction of the U6 snRNA with the Lsm2-8 protein complex, causes defective RNA splicing, and triggers massive DNA damage and subsequent cell death. Splicing defects and cell death can be mitigated by recombinant U6 snRNA containing an oligo(U) tail. We propose that the TUT1-catalyzed oligo(U) tail is essential for splicing and cell proliferation. Further modification of this oligo(U) tail by USB1 is ubiquitous but only functionally required in specific cell types. - Source: PubMed
Publication date: 2026/04/09
Fang YinQiu TongLuo HongWang YanYang ChaoWang MinDai QianZheng WenyueYin RutieXiao XueLi Qintong - Ovarian cancer (OC), a common fatal malignancy in women, has a poor prognosis. RNA modifications are associated with the development of OC. In this study, we aimed to identify and verify RNA modifications-related prognostic genes in OC by integrating bulk and single-cell RNA sequencing (scRNA-seq) data. - Source: PubMed
Publication date: 2025/05/20
Wang ShaoyuZheng QiaomeiChen Lihong - The caudal neurosecretory system (CNSS), present in all jawed vertebrates, except sarcopterygians, is considered a major site of urotensin II (UII) secretion. UII, a 12-amino acid peptide with a conserved hexapeptide ring structure, is also secreted by other tissues and found in sarcopterygians. UII has been associated with endocrine regulation, osmoregulation, and several pathophysiological conditions. In this study, CDS of GIFT Nile tilapia (Oreochromis niloticus) UII (tUII) and its receptors UT1 (tUT1) and UT2 (tUT2) were cloned from the CNSS and cerebellum, respectively. Phylogenetic analysis indicated that tUII, tUT1, and tUT2 shared a high homology with the ones of cichlid species, Haplochromis burtoni and Neolamprologus brichardi. Despite variations in precursor peptide sequences, the core sequence of the mature UII peptide remains highly conserved. tUII was predominantly expressed in the CNSS, while tUT1 and tUT2 were widely distributed in the central nervous system (CNS) and peripheral tissues of male and female tilapia. Functional studies revealed that synthetic tUII significantly activated luciferase activity in HEK293T cells transiently transfected with pNFAT-TA-Luc vectors and tUT1 or tUT2. In vitro studies in male GIFT Nile tilapia showed that tUII stimulated mRNA expression of gnrh1, gnrh2, and gnrh3 in a dose-dependent manner by brain fragments, as well as fshβ, lhβ, and gthα by primary culture of pituitary cells. Furthermore, tUII promoted the expression of gnrhr1, gnrhr2, and gnrhr3 in pituitary cells and stimulated mRNA levels of fshr, lhr, arα, cyp11b2, and dmrt1 in testicular tissue. All these stimulatory effects of tUII on gene expression mentioned above were blocked by the non-selective UT antagonist urantide, suggesting for the first time that the actions of tUII were mediated via tUT1 or tUT2. In addition, tUII could significantly stimulate the secretion of testosterone by testis fragments. Taken together, these results suggest that tUII may play a role in reproductive regulation in male GIFT Nile tilapia. - Source: PubMed
Publication date: 2025/04/01
Bai YingZhang XushengYu XiaozhengLian YingyingLai KingwaiChen XiaoxiaLi WenshengSun Caiyun - Pancreatic ductal adenocarcinoma (PDAC) is highly aggressive and lacks effective therapeutic options. Cancer cells frequently become more dependent on splicing factors than normal cells due to increased rates of transcription. Terminal uridylyltransferase 1 (TUT1) is a specific terminal uridylyltransferase for U6 small nuclear RNA (snRNA), which plays a catalytic role in the spliceosome. In this study, we found that TUT1 was required for the survival of PDAC cells but not for normal pancreatic cells. In PDAC cells, the uridylylation activity of TUT1 promoted U4/U6.U5 tri-small nuclear ribonucleoprotein particles (snRNP) assembly by facilitating the binding of LSM proteins to U6 snRNA and subsequent tri-snRNP assembly. PDAC cells required higher amounts of U4/U6.U5 tri-snRNP to efficiently splice pre-mRNA with weak splice sites to support the high transcriptional output. Depletion of TUT1 in PDAC cells resulted in inefficient splicing of exons in a group of highly expressed RNAs containing weak splice sites, thereby resulting in the collapse of an mRNA processing circuit and consequently dysregulating splicing required by PDAC cells. Overall, this study unveiled an interesting function of TUT1 in regulating splicing by modulating U4/U6.U5 tri-snRNP levels and demonstrated a distinct mechanism underlying splicing addiction in pancreatic cancer cells. Significance: The higher amounts of U6 snRNA in tri-snRNP pools in pancreatic cancer cells compared with normal cells confers sensitivity to TUT1 inhibition, which mimics tri-snRNP inhibition and causes pancreatic cancer cell senescence. - Source: PubMed
Guo ZiweiHuang JunranLu Zhi JShi YongshengDavid Charles JChen Mo