Association of Purα and E2F-1 suppresses transcriptional activity of E2F-1
| العنوان: | Association of Purα and E2F-1 suppresses transcriptional activity of E2F-1 |
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| المؤلفون: | Natalia Shcherbik, Anna Tretiakova, Mondira Kundu, Nune Darbinian, Kamel Khalili, Antonio Giordano, Gary L. Gallia |
| المصدر: | Oncogene. 18:6398-6402 |
| بيانات النشر: | Springer Science and Business Media LLC, 1999. |
| سنة النشر: | 1999 |
| مصطلحات موضوعية: | Cancer Research, Transcription, Genetic, Immunoprecipitation, Recombinant Fusion Proteins, DNA, Single-Stranded, Cell Cycle Proteins, Biology, Transfection, Retinoblastoma Protein, DNA-binding protein, Cell Line, S Phase, chemistry.chemical_compound, Genes, Reporter, Consensus Sequence, Genetics, Humans, Binding site, Cyclic AMP Response Element-Binding Protein, Promoter Regions, Genetic, E2F, Molecular Biology, Gene, Transcription factor, Binding Sites, Cell-Free System, Cell Cycle, Cell cycle, Molecular biology, E2F Transcription Factors, DNA-Binding Proteins, Tetrahydrofolate Dehydrogenase, chemistry, Astrocytes, biological phenomena, cell phenomena, and immunity, Carrier Proteins, Transcription Factor DP1, E2F1 Transcription Factor, DNA, Protein Binding, Retinoblastoma-Binding Protein 1, Transcription Factors |
| الوصف: | Protein-protein interaction can play an important role in the control of several biological events including gene transcription, replication and cell proliferation. E2F-1 is a DNA-binding transcription factor which, upon interaction with its target DNA sequence, induces expression of several S phase specific genes allowing progression of the cell cycle. Evidently, the activity of this protein is modulated by its cellular partner, pRb, which in the hypophosphorylated form, binds to E2F-1 and inactivates its transcriptional ability. In this study, we have demonstrated that expression of a sequence-specific single-stranded DNA binding protein, Pur alpha, in cells decreases the ability of E2F-1 to exert its transcriptional activity upon the responsive promoter derived from DHFR. Results from band shift experiments revealed that while Pur alpha does not recognize the double-stranded DNA fragment containing the E2F-1 binding site, it has the ability to inhibit E2F-1 interaction with its target DNA sequence. Results from GST pull-down assays and the combined immunoprecipitation/Western blot analysis of nuclear extracts revealed a direct association of E2F-1 with Pur alpha in the absence of the DNA molecule containing the E2F-1 binding site. The association of Pur alpha with E2F-1 may increase the stability of E2F-1, as a higher level of E2F-1 was detected in cells coexpressing Pur alpha and E2F-1. The importance of these observations with respect to the role of Pur alpha in the control of cell cycle progression is discussed. |
| تدمد: | 1476-5594 0950-9232 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31849436abb0c66064deea816b1a7efeTest https://doi.org/10.1038/sj.onc.1203011Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....31849436abb0c66064deea816b1a7efe |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14765594 09509232 |
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