Identification of an RNA binding specificity for the potential splicing factor TLS (Q28138875)

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M Hallier

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L Delva

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C Orvain

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I Gallais

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J Marie

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F Moreau-Gachelin

Journal of Biological Chemistry

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language of work or name

English

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publication date

2 March 2001

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published in

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volume

276

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page(s)

6807-16

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issue

9

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cites work

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Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours

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The Ewing's sarcoma EWS/FLI-1 fusion gene encodes a more potent transcriptional activator and is a more powerful transforming gene than FLI-1

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A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP

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DNA-binding and transcriptional activation properties of the EWS-FLI-1 fusion protein resulting from the t(11;22) translocation in Ewing sarcoma

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Dual transforming activities of the FUS (TLS)-ERG leukemia fusion protein conferred by two N-terminal domains of FUS (TLS).

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Male sterility and enhanced radiation sensitivity in TLS(-/-) mice

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Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death.

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Human POMp75 is identified as the pro-oncoprotein TLS/FUS: both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation

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Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation

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EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes.

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TLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis

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TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors

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The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS

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A 69-kD protein that associates reversibly with the Sm core domain of several spliceosomal snRNP species.

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Association of SARFH (sarcoma-associated RNA-binding fly homolog) with regions of chromatin transcribed by RNA polymerase II.

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Cabeza, a Drosophila gene encoding a novel RNA binding protein, shares homology with EWS and TLS, two genes involved in human sarcoma formation

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Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm

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Identification of a human protein that recognizes the 3' splice site during the second step of pre-mRNA splicing

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Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing

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TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins

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The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb

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RNA secondary structure repression of a muscle-specific exon in HeLa cell nuclear extracts.

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Production of erythropoietin-like activity by a murine erythroleukemia cell line

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An intronic (A/U)GGG repeat enhances the splicing of an alternative intron of the chicken beta-tropomyosin pre-mRNA

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Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs

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Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein

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RNA splicing specificity determined by the coordinated action of RNA recognition motifs in SR proteins

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The splicing factor BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC.

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Determinants of SR protein specificity.

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G triplets located throughout a class of small vertebrate introns enforce intron borders and regulate splice site selection

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Functional recognition of the 3' splice site AG by the splicing factor U2AF35.

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Fusion of the FUS gene with ERG in acute myeloid leukemia with t(16;21)(p11;q22)

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Molecular cloning and subcellular localisation of the snRNP-associated protein 69KD, a structural homologue of the proto-oncoproteins TLS and EWS with RNA and DNA-binding properties

21 January 2018

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Normal and mutant human β-globin pre-mRNAs are faithfully and efficiently spliced in vitro

21 January 2018

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Nucleolin is a sequence-specific RNA-binding protein: characterization of targets on pre-ribosomal RNA

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21 January 2018

Identifiers

DOI

10.1074/JBC.M008304200

1 reference

Consolidated OpenCitations Corpus – April 2017

4551804

4551804

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference