Ask about this productRelated genes to: NHP2L1 antibody
- Gene:
- SNU13 NIH gene
- Name:
- small nuclear ribonucleoprotein 13
- Previous symbol:
- SSFA1, NHP2L1
- Synonyms:
- FA-1, SPAG12, SNRNP15-5, 15.5K
- Chromosome:
- 22q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-06-14
- Date modifiied:
- 2019-04-23
Related products to: NHP2L1 antibody
Related articles to: NHP2L1 antibody
- Pre-mRNA splicing is carried out by the spliceosome, a dynamic complex of five small nuclear ribonucleoprotein particles (snRNPs). Several genetic screens have been conducted in to identify pre-mRNA splicing mutants and spliceosome components However, some pre-mRNA splicing mutants have yet to be assigned to a gene and in certain cases, the mutations within genes have not been identified and phenotypes compared. Here, we have identified new mutations in the U4/U6.U5 tri-snRNP component and assigned and mutants to and , respectively, revealing roles for these factors in pre-mRNA splicing. - Source: PubMed
Publication date: 2026/03/17
Nicholas Laurel LSuo FangHanna Sarah MDu Li-LinGould Kathleen L - Multicellular tissues require continuous optimization to maintain their integrity by eliminating viable but unfit cells through cell competition. During this process, unfit "loser" cells upregulate the C/EBP-family transcription factor Xrp1, which drives their elimination and thus determines cellular fitness. However, the mechanism underlying Xrp1 upregulation remains unclear. Here, we show that Xrp1 is upregulated through a post-transcriptional mechanism mediated by ribosomal protein S12 (RpS12). Although Xrp1 mRNA is abundantly expressed in wild-type cells, its translation is repressed by an upstream open reading frame (uORF) in the 5' UTR. In unfit cells, RpS12 promotes splicing-mediated skipping of the uORF-containing exon, enabling the use of an alternate start codon that produces a short Xrp1 isoform triggering cell death. Structural analysis reveals strong similarity between RpS12 and the spliceosomal component SNU13, suggesting a direct role for RpS12 in alternative splicing. Our findings provide mechanistic insight into how cellular fitness is determined. - Source: PubMed
Publication date: 2026/03/26
Kakemura BungoKanda HiroshiMatsumoto RyoUeda ShioriYasuhara SatoshiNagata RinaTaniguchi KiichiroKondo ShuMiyoshi KeitaKobayashi TomoeTakeuchi KazuhiroSaito KuniakiMatsuyama MakotoMurakawa YasuhiroIgaki Tatsushi - Ribosomes are ribonucleoproteins that are responsible for protein synthesis. They consist of ribosomal proteins and ribosomal RNAs (rRNAs). Pre-rRNAs are co-transcriptionally processed and chemically modified. The 2'-O-methylation of rRNAs is guided by box C/D small nucleolar ribonucleoprotein particles (snoRNPs), which are composed of a box C/D snoRNA and the core proteins NOP56, NOP58, SNU13, and the methyltransferase fibrillarin. Catalytically active box C/D snoRNPs function in nucleoli. We performed trio whole-exome sequencing in a proband with a severe neurodevelopmental disorder including global developmental delay, microcephaly, seizures, and ophthalmological and brain abnormalities and his healthy parents and identified the homozygous synonymous variant c.516G>A; p.Leu172= in NOP58. In fibroblasts of the proband, we demonstrated skipping of exon 7 in most NOP58 mRNAs, while ∼20% canonically spliced NOP58 transcripts were detected in the proband compared with control cells. NOP58 protein levels were reduced to ∼12% in proband cells that concomitantly reduced fibrillarin levels. Analysis of nucleoli in proband-derived fibroblasts revealed changes in the number of nucleolar condensates and in nucleolar morphology. We found reduced levels of three box C/D snoRNAs required for 2'-O-methylation and of one box C/D snoRNA important for 2'-O-methylation and pre-rRNA processing. Analysis of pre-rRNA maturation by RT-qPCR revealed increased 45S and 21S pre-rRNA levels, whereas the amplification signal for the 47S, 32S, and 26S pre-rRNAs was substantially decreased in proband compared with control cells. Together, our data unveil that the homozygous NOP58 variant c.516G>A represents a hypomorphic allele and underlies the neurodevelopmental phenotype in the proband, likely by impairing pre-rRNA maturation. - Source: PubMed
Publication date: 2025/12/11
Bonde Loisa DHolling TessAlawi MalikEl Beheiry Ahmed AMir Hassani ZabihBachand FrançoisAbdelrazek Ibrahim MKutsche Kerstin - The spliceosome is a large ribonucleoprotein complex that regulates pre-mRNA splicing and has been an intriguing target for drug discovery. Essential to the assembly of the spliceosome are the small nuclear RNAs (snRNAs), which form RNA-RNA and RNA-protein interactions in the intact spliceosome and during its assembly. Here, we study the yeast U4/U6 snRNA assembly and report the rapid discovery of small molecule K-turn ligands via parallel small molecule microarray (SMM) screening of multiple related RNA constructs. For hit validation, biophysical analyses were conducted to confirm the binding and effects on thermodynamic stability and of RNA structure. One analog of the hit molecule () exhibited improved affinity towards the yeast U4/U6 snRNA (K = 3.9 ± 2.2 μM). The specific interaction between 22 and the K-turn region was studied experimentally using deltaSHAPE and with MD simulations. Moreover, this molecule was found to inhibit the binding of the U4 to Snu13 in biochemical assays (IC = 3.2 ± 0.4 μM). This work reports new ligands for the U4 snRNA and reveals that a multiplexed, structure-based approach can be used to identify small molecules that bind to specific regions of complex RNAs. - Source: PubMed
Publication date: 2025/10/11
Yang MoParmar ShaifalyBalaratnam SumirthaBume Desta DPrestwood Peri RKasprzak Wojciech KSchneekloth John S - Ovarian cancer often develops resistance to conventional therapies, hampering their effectiveness. Here, using ex vivo paired ovarian cancer ascites obtained before and after chemotherapy and in vitro therapy-induced secretomes, we show that molecules secreted by ovarian cancer cells upon therapy promote cisplatin resistance and enhance DNA damage repair in recipient cancer cells. Even a short-term incubation of chemonaive ovarian cancer cells with therapy-induced secretomes induces changes resembling those that are observed in chemoresistant patient-derived tumor cells after long-term therapy. Using integrative omics techniques, we find that both ex vivo and in vitro therapy-induced secretomes are enriched with spliceosomal components, which relocalize from the nucleus to the cytoplasm and subsequently into the extracellular vesicles upon treatment. We demonstrate that these molecules substantially contribute to the phenotypic effects of therapy-induced secretomes. Thus, SNU13 and SYNCRIP spliceosomal proteins promote therapy resistance, while the exogenous U12 and U6atac snRNAs stimulate tumor growth. These findings demonstrate the significance of spliceosomal network perturbation during therapy and further highlight that extracellular signaling might be a key factor contributing to the emergence of ovarian cancer therapy resistance. - Source: PubMed
Publication date: 2024/06/19
Shender Victoria OAnufrieva Ksenia SShnaider Polina VArapidi Georgij PPavlyukov Marat SIvanova Olga MMalyants Irina KStepanov Grigory AZhuravlev EvgeniiZiganshin Rustam HButenko Ivan OBukato Olga NKlimina Ksenia MVeselovsky Vladimir AGrigorieva Tatiana VMalanin Sergey YAleshikova Olga ISlonov Andrey VBabaeva Nataliya AAshrafyan Lev AKhomyakova ElenaEvtushenko Evgeniy GLukina Maria MWang ZixiangSilantiev Artemiy SNushtaeva Anna AKharlampieva Daria DLazarev Vassili NLashkin Arseniy IArzumanyan Lorine KPetrushanko Irina YuMakarov Alexander ALebedeva Olga SBogomazova Alexandra NLagarkova Maria AGovorun Vadim M