前胸腺素α与CREB结合蛋白相互作用并增强转录。
Prothymosin alpha interacts with the CREB-binding protein and potentiates transcription.
作者信息
Karetsou Zoe, Kretsovali Adroniki, Murphy Carol, Tsolas Orestes, Papamarcaki Thomais
机构信息
Laboratory of Biological Chemistry, University of Ioannina Medical School, 45110 Ioannina, Greece.
出版信息
EMBO Rep. 2002 Apr;3(4):361-6. doi: 10.1093/embo-reports/kvf071. Epub 2002 Mar 15.
Abstract
Prothymosin alpha (ProTalpha) is a histone H1-binding protein localized in sites of active transcription in the nucleus. We report here that ProTalpha physically interacts with the CREB-binding protein (CBP), which is a versatile transcription co-activator. Confocal laser scanning microscopy reveals that ProTalpha partially colocalizes with CBP in discrete subnuclear domains. Using transient transfections, we show that ProTalpha synergizes with CBP and stimulates AP1- and NF-kappaB-dependent transcription. Furthermore, overexpression of ProTalpha enhances the transactivation potential of CBP. These findings reveal a new function for ProTalpha in transcription activation, probably through CBP-mediated recruitment to different promoters.
摘要
前胸腺素α（ProTα）是一种与组蛋白H1结合的蛋白质，定位于细胞核中活跃转录的位点。我们在此报告，ProTα与CREB结合蛋白（CBP）发生物理相互作用，CBP是一种多功能转录共激活因子。共聚焦激光扫描显微镜显示，ProTα与CBP在离散的核内亚结构域部分共定位。通过瞬时转染，我们发现ProTα与CBP协同作用并刺激AP1和NF-κB依赖性转录。此外，ProTα的过表达增强了CBP的反式激活潜能。这些发现揭示了ProTα在转录激活中的新功能，可能是通过CBP介导招募到不同的启动子。
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