Sequence-Specific Binding of Poly(ADP-Ribose) Polymerase-1 to the Human T Cell Leukemia Virus Type-I Tax Responsive Element
| Autor: | Cynthia M. Simbulan-Rosenthal, Ellen F. Hildebrandt, Zhan Zhang, Mark G. Anderson |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Gene Expression Regulation
Viral Transcription Genetic HMG-box Poly ADP ribose polymerase Tax PARP-1 Biology Response Elements Cell Line Mice chemistry.chemical_compound Virology Coactivator Animals TxRE DNA binding Promoter Regions Genetic Transcription factor Human T-lymphotropic virus 1 CREB Promoter Gene Products tax DNA-binding domain HTLV-I Molecular biology coactivator DNA binding site chemistry Poly(ADP-ribose) Polymerases transcription Gene Deletion DNA |
| Zdroj: | Virology. 296(1):107-116 |
| ISSN: | 0042-6822 |
| DOI: | 10.1006/viro.2002.1385 |
| Popis: | We have previously identified poly(ADP-ribose) polymerase-1 (PARP-1) as a coactivator for the human T cell leukemia virus type I (HTLV-I) transcription activator Tax. While PARP-1 is believed to contribute to DNA repair, PARP-1 has been described as a coactivator for other transcription factors. Recent evidence suggests that PARP-1 forms complexes on cellular promoters, so we investigated PARP-1 complexes on the HTLV-I Tax responsive elements (TxREs) using an end-blocked DNA binding assay. We observed sequence-specific binding of PARP-1 to the TxREs. The DNA binding domain of PARP-1 was fused to the transcriptional activation domain of VP16, and this fusion protein activated the HTLV-I promoter in a TxRE-dependent manner. Internal, sequence-specific binding of PARP-1 to DNA provides a mechanism for transcriptional regulation of the HTLV-I promoter. The mechanism of PARP-1 function in the HTLV-I system may have common mechanistic steps with other cellular promoters, including the formation of active complexes on the promoter. |
| Databáze: | OpenAIRE |
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