Comment on: Tan AY, et al. Proc Natl Acad Sci USA 2012; 109:6030-5.
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DNA G-Quadruplex-Binding Protein Developed Using the RGG Domain of Translocated in Liposarcoma/Fused in Sarcoma Inhibits Transcription of .
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Graduate School of Science and Technology, Shizuoka University, 836 Ohya, Suruga, Shizuoka 422-8529, Japan.
The G-quadruplexes (G4s) in the genome are important drug targets because they regulate gene expression and the genome structure. Several small molecules that bind the G4 have been developed, but few artificial G4 binding proteins have been reported. We previously reported a novel DNA G4 binding protein (RGGF) engineered using the Arg-Gly-Gly repeat (RGG) domain of TLS (translocated in liposarcoma), also known as FUS (fused in sarcoma) protein (TLS/FUS).
View Article and Find Full Text PDFTLS/FUS-ERG fusion gene in acute leukemia and myelodysplastic syndrome evolved to acute leukemia: report of six cases and a literature review.
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Department of Hematology, The First Hospital of China Medical University, Shenyang, Liaoning, China.
To investigate the pathogenesis and the refractory/relapse mechanisms in patients with t(16;21)(p11;q22), we retrospectively analyzed the clinical data of six cases in our hospital and sixty-two cases reported in the literature. Among the patients in our hospital, five cases were diagnosed as acute leukemia, and one was myelodysplastic syndrome evolved to acute myeloid leukemia, harboring TLS/FUS-ERG fusion gene; all the cases were detected t(16;21)(p11;q22) translocation, and five cases showed additional chromosomal abnormalities. We firstly report a novel three-way translocation t(11;16;21)(q13;p11;q22), which may affect the prognosis of leukemia with TLS-ERG fusion gene because this patient shows a more satisfactory treatment effect and deeper remission.
View Article and Find Full Text PDFmA Modified Short RNA Fragments Inhibit Cytoplasmic TLS/FUS Aggregation Induced by Hyperosmotic Stress.
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Division of Biomedical Sciences, Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi, Saitama 350-1241, Japan.
Translocated in LipoSarcoma/Fused in Sarcoma (TLS/FUS) is a nuclear RNA binding protein whose mutations cause amyotrophic lateral sclerosis. TLS/FUS undergoes LLPS and forms membraneless particles with other proteins and nucleic acids. Interaction with RNA alters conformation of TLS/FUS, which affects binding with proteins, but the effect of mA RNA modification on the TLS/FUS-RNA interaction remains elusive.
View Article and Find Full Text PDFRare and favorable prognosis of pediatric acute lymphoblastic leukemia with TLS-ERG fusion gene: Case report with long-term follow-up and review of literature.
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In the study of acute myeloid leukemia (AML), TLS-ERG (also called FUS-ERG or TLS/FUS-ERG) was found to be closely associated with extramedullary disease (EMD), with very poor prognosis. However, the occurrence of TLS-ERG in acute lymphoblastic leukemia (ALL) is very rare. Till date, only 20 cases of ALL with TLS-ERG gene have been reported, of which six are children.
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Division of Gene Structure and Function, Research Center for Genomic Medicine, Saitama Medical University, Hidaka-shi, Saitama 350-1241, Japan. Electronic address:
Article Synopsis
- - The study investigates a long noncoding RNA (602-nt) linked to the cyclin D1 gene that is affected by osmotic stress and interacts with the RNA-binding protein TLS/FUS, which plays a role in inhibiting its expression.
- - Osmotic stress leads to changes in RNA and protein methylation levels, particularly reducing mA (N6-methyladenosine) methylation of the long noncoding RNA and arginine methylation of TLS, influencing their interaction and extending the RNA's lifespan.
- - Experimental manipulation, like knockdown of methylation enzymes and deletion of mA sites, disrupts interactions affecting cell cycle progression, showing that mA modification is key for regulating gene expression and potentially controlling
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