Chiarugi V, Cinelli M, Magnelli L
Laboratory of Molecular Biology, University of Florence, Italy.
Oncol Res. 1998;10(2):55-7.
Three fundamental domains are conventionally distinguished on the p53 molecule: an NH2 domain involved in transcription, a central core domain involved in specific DNA binding to the consensus sequences, and a carboxy-terminal domain of about 30 amino acids working as a basic regulatory domain, exhibiting aspecific DNA binding, tetramerization, and nuclearization. The presence of an unmodified carboxy-terminus does not allow the specific transactivation transcriptional function of the p53 protein. Therefore, for the activation of the protein function the carboxy-terminus must be modified. In the present commentary we discuss the role of two covalent modification events occurring at the carboxy-terminus, namely phosphorylation and acetylation, as well as the specific role of these events in the functional regulation of p53 molecule.
传统上，p53分子可分为三个基本结构域：参与转录的氨基末端结构域、参与与共有序列特异性DNA结合的中央核心结构域，以及约30个氨基酸的羧基末端结构域，作为基本调节结构域，具有非特异性DNA结合、四聚化和核定位功能。未修饰的羧基末端的存在不允许p53蛋白发挥特异性反式激活转录功能。因此，为激活蛋白功能，羧基末端必须被修饰。在本评论中，我们讨论了发生在羧基末端的两种共价修饰事件，即磷酸化和乙酰化的作用，以及这些事件在p53分子功能调节中的具体作用。
