ArticleThe Journal of biological chemistry2012
Tudor staphylococcal nuclease (Tudor-SN) participates in small ribonucleoprotein (snRNP) assembly via interacting with symmetrically dimethylated Sm proteins.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 75 citations in OpenAlex.
- Beyond VEGF: AEG-1/MTDH as a Systems-Level Orchestrator of Angiogenesis in Hepatocellular Carcinoma.Cells · 2026Review
- SREBF1-mediated SND1 transcriptional activation promotes prostate cancer progression via MTDH interaction through the SESN2/AMPK/mTOR axis.Journal of translational medicine · 2025Article
- The Early Evolution of Tudor Genes in Holozoa and How Their Distribution Was Influenced by Life History Traits in Metazoa.Genome biology and evolution · 2025Article
- Loss of the methylarginine reader function of SND1 confers resistance to hepatocellular carcinoma.The Biochemical journal · 2023Article
- Effectors and effects of arginine methylation.Biochemical Society transactions · 2023Article
- Circular RNA METTL9 contributes to neuroinflammation following traumatic brain injury by complexing with astrocytic SND1.Journal of neuroinflammation · 2023Article
- Bidirectional Functional Effects ofMicroorganisms · 2022Review
- Exonic splicing code and protein binding sites for calcium.Nucleic acids research · 2022Article
- Impact of hepatocyte-specific deletion of staphylococcal nuclease and tudor domain containing 1 (SND1) on liver insulin resistance and acute liver failure of mice.Bioengineered · 2021Article
- Multifunctional Role of Astrocyte Elevated Gene-1 (AEG-1) in Cancer: Focus on Drug Resistance.Cancers · 2021Review
- The Role of the PRMT5-SND1 Axis in Hepatocellular Carcinoma.Epigenomes · 2021Article
- Astrocyte elevated gene-1 (AEG-1): A key driver of hepatocellular carcinoma (HCC).Advances in cancer research · 2021Review
- Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1.Frontiers in molecular biosciences · 2021Article
- Modified base-binding EVE and DCD domains: striking diversity of genomic contexts in prokaryotes and predicted involvement in a variety of cellular processes.BMC biology · 2020Article
- Article
- Contribution of alternative splicing to breast cancer metastasis.Journal of cancer metastasis and treatment · 2019Article
- Oncoprotein Tudor-SN is a key determinant providing survival advantage under DNA damaging stress.Cell death and differentiation · 2018Article
- Tudor staphylococcal nuclease is a structure-specific ribonuclease that degrades RNA at unstructured regions during microRNA decay.RNA (New York, N.Y.) · 2018Article
- Insights IntoFrontiers in oncology · 2018Review
- SND1 acts as an anti-apoptotic factor via regulating the expression of lncRNA UCA1 in hepatocellular carcinoma.RNA biology · 2018Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human Tudor staphylococcal nuclease (Tudor-SN) is composed of four tandem repeats of staphylococcal nuclease (SN)-like domains, followed by a tudor and SN-like domain (TSN) consisting of a central tudor flanked by two partial SN-like sequences. The crystal structure of the tudor domain displays a conserved aromatic cage, which is predicted to hook methyl groups. Here, we demonstrated that the TSN domain of Tudor-SN binds to symmetrically dimethylarginine (sDMA)-modified SmB/B' and SmD1/D3 core proteins of the spliceosome. We demonstrated that this interaction ability is reduced by the methyltransferase inhibitor 5-deoxy-5-(methylthio)adenosine. Mutagenesis experiments indicated that the conserved amino acids (Phe-715, Tyr-721, Tyr-738, and Tyr-741) in the methyl-binding cage of the TSN domain are required for Tudor-SN-SmB interaction. Furthermore, depletion of Tudor-SN affects the association of Sm protein with snRNAs and, as a result, inhibits the assembly of uridine-rich small ribonucleoprotein mediated by the Sm core complex in vivo. Our results reveal the molecular basis for the involvement of Tudor-SN in regulating small nuclear ribonucleoprotein biogenesis, which provides novel insight related to the biological activity of Tudor-SN.
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