Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase

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Abstract

We isolated several clones from a matchmaker two-hybrid system human lymphocyte cDNA library using an automodification domain of poly(ADP-ribose) synthetase (PARS) as a probe. A DNA sequence (~1 kbp) of the clone was identical to part of the Oct-1 DNA sequence. We then constructed either a His-tagged or GST fusion protein of the inserted cDNA from the clone and the fusion protein,vas shown to interact with PARS by far-Western blot analysis and coprecipitation with affinity resin. Furthermore, the His-tagged Oct-1/POU-homeo fusion protein interacted weakly with the octamer motif of the DRa promoter and the addition of PARS fusion protein greatly increased the DNA binding activity. These results suggest that PARS interacts with Oct-1 and stabilizes the binding of Oct-1 to the octamer motif.

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Nie, J., Sakamoto, S., Song, D., Qu, Z., Ota, K., & Taniguchi, T. (1998). Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase. FEBS Letters, 424(1–2), 27–32. https://doi.org/10.1016/S0014-5793(98)00131-8

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