Coactivator p100 protein enhances histone acetyltransferase activity of CBP

• 作 者: OLLI SILVENNOINEN
• 机 构: Laboratory of Molecular Immunology Institute of Medical Technology University of Tampere,Finland,
• 出 处: Journal of Microbiology and Immunology
• 发表日期: 2006年01期
• 关键词: staphylococcal thereafter alone acetyl sufficiently CREB histone bridged subunit

Human p100 protein consists of four repeated domains of staphylococcal nuclease (SN)-like domain, as well as a tudor (TD) domain thereafter. We have previously shown that the SN-like domain of p100 interacted with STAT6 and the large subunit of RNA pol II , resulting in the enhancement of STAT6-mediated gene transcriptional activation. Here, we show that SN-like domain also interacted with CREB binding protein (CBP) and directly enhanced the acetyl transferase activity of CBP on his tone. On the other hand, overexpression of CBP alone had no ability to significantly increase STAT6 dependent transcriptional activation, however, together with p100 protein, sufficiently enhanced the activation of transcription which was in line with the previous result that p100 protein bridged STAT6 with CBP.

Human p100 protein consists of four repeated domains of staphylococcal nuclease (SN) -like domain, as well as a tudor (TD) domain after. We have previously shown that the SN-like domain of p100 interacted with STAT6 and the large subunit of RNA pol II, resulting in the enhancement of STAT6-mediated gene transcriptional activation. Here, we show that SN-like domain also interacts with CREB binding protein (CBP) and directly enhanced the acetyl transferase activity of CBP on his tone. , overexpression of CBP alone had no ability to significantly increase STAT6 dependent transcriptional activation, however, together with p100 protein, enhanced enhanced the activation of transcription which was in line with the previous result that p100 protein bridged STAT6 with CBP.