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. © 2002 Elsevier Science (USA).
CITATION STYLE
Zhang, Z., Hildebrandt, E. F., Simbulan-Rosenthal, C. M., & Anderson, M. G. (2002). Sequence-specific binding of poly(ADP-ribose) polymerase-1 to the human T cell leukemia virus type-I Tax responsive element. Virology, 296(1), 107–116. https://doi.org/10.1006/viro.2002.1385
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