Johnston H, Kneer J, Chackalaparampil I, Yaciuk P, Chrivia J
Department of Pharmacological and Physiological Sciences, Saint Louis University, Saint Louis, Missouri 63104, USA.
J Biol Chem. 1999 Jun 4;274(23):16370-6. doi: 10.1074/jbc.274.23.16370.
The ability of cAMP response-element binding protein (CREB)-binding protein (CBP) to function as a co-activator for a number of transcription factors appears to be mediated by its ability to act as a histone acetyltransferase and through its interaction with a number of other proteins (general transcription factors, histone acetyltransferases, and other co-activators). Here we report that CBP also interacts with a novel ATPase termed Snf2-Related CBP Activator Protein (SRCAP). Consistent with this activity, SRCAP contains the conserved ATPase domain found within members of the Snf2 family. Transfection experiments demonstrate that SRCAP is able to activate transcription when expressed as a Gal-SRCAP chimera and that SRCAP also enhances the ability of CBP to activate transcription. The adenoviral protein E1A was found to disrupt interaction between SRCAP and CBP possibly representing a mechanism for E1A-mediated transcriptional repression.
环磷酸腺苷反应元件结合蛋白（CREB）结合蛋白（CBP）作为多种转录因子的共激活因子发挥作用的能力，似乎是由其作为组蛋白乙酰转移酶的能力以及通过与许多其他蛋白质（通用转录因子、组蛋白乙酰转移酶和其他共激活因子）的相互作用介导的。在此我们报告，CBP还与一种名为Snf2相关CBP激活蛋白（SRCAP）的新型ATP酶相互作用。与这种活性一致，SRCAP含有Snf2家族成员中发现的保守ATP酶结构域。转染实验表明，当作为Gal-SRCAP嵌合体表达时，SRCAP能够激活转录，并且SRCAP还增强了CBP激活转录的能力。发现腺病毒蛋白E1A会破坏SRCAP和CBP之间的相互作用，这可能代表了E1A介导的转录抑制机制。
