Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.6 (RNA polymerase)
 34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cells of the line 3BM-78 derived from murine bone marrow cells infected in vitro with polycythemic Friend leukemia virus (FLV-P) produce virus with spleen focus-forming activity (SFFV) and can be induced to synthesize hemoglobin. Fifteen clones, isolated from this line, have been analyzed in detail for the effect of different inducing agents (dimethyl-sulfoxide, DMSO; hexamethylene bisacetamide, HMBA; and sodium butyrate, SB) on the synthesis of hemoglobin and virus at the clonal level. All the clones proved to be inducible with one or more of the agents, but the degree of the response depended on the type and concentration of the agent used. In general, the effectiveness of the agent--within the usual range of concentration for induction--both for hemoglobin and for virus synthesis, was in the order HMBA greater than DMSO greater than SB. Reverse transcriptase activity was, however, more easily induced than hemoglobin synthesis in that stimulation was seen at lower concentrations of the same inducing agent. This clonal analysis confirmed that virus and hemoglobin production are regulated independently in these erythroleukemic cells chronically infected with FLV-P.
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PMID:Variations in the response of cloned murine friend erythroleukemia cells to different inducers. 616 76

The amount of S-II, a protein specifically stimulating RNA polymerase II, was measured in various mouse organs by a micro complement fixation assay. The amount was almost the same in brain, liver, kidney, spleen, and Ehrlich ascites tumor cells on the basis of DNA, being about 3.8 micrograms/mg DNA, which corresponds to 3.6 X 10(5) molecules/cell. However, the amount of S-II decreased greatly during erythro-differentiation of Friend leukemia cells and no S-II was detected matured erythrocytes.
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PMID:Measurement of a stimulatory protein of RNA polymerase II in various mouse organs by the complement fixation test. 746 90

The human p53 tumor suppressor gene product can activate transcription by RNA polymerase II in the yeast, Saccharomyces cerevisiae, as well as in human cells. Several viral transcriptional activator proteins have been shown to directly contact TBP, the TATA box-binding subunit of the general initiation factor, TFIID. In this report, we use protein affinity chromatography to show that the cellular transcription factor, p53, interacts directly and specifically with yeast TBP. The TBP binding domain of p53 was localized to its N-terminal 73 amino acids. This highly acidic portion of p53 functions as a transcriptional activation domain and is deleted in some tumors induced by the Friend leukemia virus. A human tumor-derived oncogenic point mutation of p53, which lies outside the activation domain of p53, but reduces its ability to activate transcription, greatly reduced the ability of p53 to bind yeast TBP in vitro. This mutation probably affects the overall conformation of the protein and indirectly interferes with the ability of p53 to contact TBP and activate transcription. In contrast, a mutated oncogenic form of p53 that is unaffected in its ability to activate transcription bound yeast TBP as well as wild type p53. The human TBP activity in a HeLa extract also bound to the activation domain of p53. Our data support a general model in which DNA-bound activator proteins activate transcription by interacting with TBP.
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PMID:Direct interaction between the transcriptional activation domain of human p53 and the TATA box-binding protein. 842 1

Ewing's sarcoma displays a characteristic chromosomal translocation that results in fusion of the N-terminal domain of the Ewing's sarcoma protein (EWS) to the C-terminal DNA-binding domain of the ETS family transcription factor Fli-1 (Friend leukemia integration-1). EWS possesses structural motifs suggesting a role in transactivation as well as RNA binding. We demonstrate that wild-type EWS protein functions as an adapter molecule coupling transcription to RNA splicing by binding to hyperphosphorylated RNA polymerase II through the N-terminal domain of EWS and recruiting serine-arginine (SR) splicing factors through the C-terminal domain of EWS. The oncogenic EWS.Fli-1 fusion protein retains the ability to bind to hyperphosphorylated RNA polymerase II but lacks the ability to recruit SR proteins because of replacement of the C-terminal domain of EWS by Fli-1. In an in vivo splicing assay, the EWS.Fli-1 fusion protein inhibits SR protein-mediated E1A pre-mRNA splicing in a dominant-negative manner. These results indicate that EWS.Fli-1 interferes with the normal function of EWS and implicate uncoupling of gene transcription from RNA splicing in the pathogenesis of Ewing's sarcoma.
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PMID:EWS.Fli-1 fusion protein interacts with hyperphosphorylated RNA polymerase II and interferes with serine-arginine protein-mediated RNA splicing. 1098