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In the present study, the interaction of human p100 protein with signal transducer and activator of transcription-6 (STAT-6) was investigated. It was proved that the staphylococcal nuclease (SN)-like and tudor (TD) domains containing in p100 protein acting as a adaptor to recruit STAT-6 to the basal transcription machinery, enhanced the STAT-6 mediated transcription activity. The interaction between STAT-6 and the p100 protein was mediated by the full-length of the SN-like domain, whereas individual fragments of SN-like domain showed no binding activity to STAT-6. In line with these results, the SN-like domain was directly engaged in the enhancement of STAT-6 mediated activation of gene transcription in vivo. Yet the TD domain had no ability to increase the transcription activation, but it was still required for the sufficient activation of transcription.
In the present study, the interaction of human p100 protein with signal transducer and activator of transcription-6 (STAT-6) was investigated. It was proved that the staphylococcal nuclease (SN) -like and tudor (TD) domains containing in p100 protein acting as a adapter to recruit STAT-6 to the basal transcription machinery, enhanced the STAT-6 mediated transcription activity. The interaction between STAT-6 and the p100 protein was mediated by the full-length of the SN-like domain, fragments of SN-like domain showed no binding activity to STAT-6. In line with these results, the SN-like domain was directly engaged in the enhancement of STAT-6 mediated activation of gene transcription in vivo. Yet the TD domain had no ability to increase the transcription activation, but it was still required for the sufficient activation of transcription.