Quèlo Isabelle, Hurtubise Mélanie, St-Arnaud René
Genetics Unit, Shriners Hospital for Children, McGill University, Montreal, Quebec, Canada.
Gene Expr. 2002;10(5-6):255-62. doi: 10.3727/000000002783992433.
alphaNAC is a transcriptional coactivator known to interact with the N-terminal activation domain of the c-Jun transcription factor. In this article, we describe the identification of the c-Jun interaction domain within the alphaNAC protein. Deletion analysis of alphaNAC indicated that the c-Jun binding site was located in the middle part of the protein, between residues 89 and 129. The deletion of the C-terminal end of alphaNAC, including the c-Jun interacting domain, induced a nuclear translocation of the mutated coactivator. Despite its presence in the nucleus, this deletion mutant did not retain the capacity to coactivate an AP-1 response. These results demonstrate that the interaction between alphaNAC and c-Jun was necessary for the potentiation of theAP-1 transcriptional activity. These data are consistent with a mechanism by which alphaNAC acts as a coactivator for c-Jun-dependent transcription by interacting with the c-Jun N-terminal activation domain.
αNAC是一种转录共激活因子，已知其可与c-Jun转录因子的N端激活结构域相互作用。在本文中，我们描述了αNAC蛋白内c-Jun相互作用结构域的鉴定。αNAC的缺失分析表明，c-Jun结合位点位于该蛋白的中部，在第89位和第129位残基之间。αNAC C端的缺失，包括c-Jun相互作用结构域，导致突变的共激活因子发生核转位。尽管该缺失突变体存在于细胞核中，但它不具备共激活AP-1反应的能力。这些结果表明，αNAC与c-Jun之间的相互作用对于增强AP-1转录活性是必需的。这些数据与一种机制一致，即αNAC通过与c-Jun N端激活结构域相互作用，作为c-Jun依赖性转录的共激活因子发挥作用。
