生物
转录因子
抄写(语言学)
P50页
突变体
效应器
遗传学
DNA
同源(生物学)
DNA结合蛋白
细胞生物学
分子生物学
基因
语言学
哲学
出处
期刊:Oncogene
[Springer Nature]
日期:1997-04-03
卷期号:14 (13): 1521-1530
被引量:10
标识
DOI:10.1038/sj.onc.1200985
摘要
Previous studies showed that the binding of p50/NFκB1 to particular κB DNA sites altered its conformation in a way that correlated with transcriptional activation. Here, we investigated the effects of protein – protein interactions on the transcriptional activity of p50. We show that the association of p50 with a mutant Rel-homology domain (RHD) defective for DNA binding led to synergistic activation of κB site-dependent transcription, whereas neither protein alone had any effect. Partial proteolytic analysis showed that the conformation of p50 in these complexes differed from that in wild-type c-Rel-RHD/p50 complexes, and correlated with activated transcription. These results suggest that the Rel-homology domain can act as an allosteric effector to promote transcription by p50/NFκB1 and that the configuration of p50 is important for its activity. This also suggests that Rel proteins can promote transcription by other Rel-family members without binding to their DNA recognition site. These studies emphasize the important role of protein – protein interactions in Rel and NFκB-mediated transcription.
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