a Institute for Cancer Genetics, Department of Pathology and Cell Biology, Herbert Irving Comprehensive Cancer Center, College of Physicians & Surgeons , Columbia University , New York , NY , USA.
Nucleus. 2017 Jul 4;8(4):360-369. doi: 10.1080/19491034.2017.1313939. Epub 2017 Apr 13.
Acetylation of non-histone proteins plays important roles in regulating protein functions but the mechanisms of action are poorly understood. Our recent study uncovered a previously unknown mechanism by which C-terminal domain (CTD) acetylation of p53 serves as a "switch" to determine the interaction between a unique group of acidic domain-containing proteins and p53, as well as revealed that acidic domains may act as a novel class of "readers" for unacetylated p53. However, the properties of acidic domain "readers" are not well elucidated yet. Here, we identified that the charge effect between acidic domain "readers" and the p53 CTD is necessary for their interaction. Both the length and the amino acid composition of a given acidic domain contributed to its ability to recognize the p53 CTD. Finally, we summarized the characteristic features of our identified acidic domains, which would distinguish this kind of "readers" from other types of acidic amino acid-containing domains.
组蛋白非乙酰化在调节蛋白质功能方面发挥着重要作用，但作用机制尚不清楚。我们最近的研究揭示了一个以前未知的机制，即 p53 的 C 端结构域（CTD）乙酰化作为一种“开关”，决定了一组独特的酸性结构域蛋白与 p53 之间的相互作用，同时还揭示了酸性结构域可能作为一类新型的“阅读器”，识别未乙酰化的 p53。然而，酸性结构域“阅读器”的特性尚未得到充分阐明。在这里，我们发现酸性结构域“阅读器”与 p53 CTD 之间的电荷效应对于它们的相互作用是必要的。给定酸性结构域的长度和氨基酸组成都有助于其识别 p53 CTD 的能力。最后，我们总结了我们鉴定出的酸性结构域的特征，这将使这种“阅读器”与其他类型的含酸性氨基酸的结构域区分开来。
