Eukaryotic genomes are maintained within DNA-protein complexes called chromatin. Post-translational modification of chromatin proteins, and especially acetylation of the core histone amino-terminal tails, has long been associated with chromatin assembly and the regulation of gene expression. It is now well accepted that an elaborate array of enzymes are responsible for posttranslational chromatin marks including acetylation and methylation among others and that together they have profound effects on gene regulation. However, this was not always the case. Here we describe the events surrounding the initial identification of GCN5 as a histone acetyltransferase from Tetrahymena thermophila and the discovery that it is an ortholog of a transcription co-activator complex in yeast. This discovery was the first to directly link a well-described transcription factor and histone modifying activity.

真核基因组维持在称为染色质的 DNA-蛋白质复合物中。染色质蛋白的翻译后修饰，尤其是核心组蛋白氨基末端尾部的乙酰化，长期以来一直与染色质组装和基因表达的调节有关。现在人们普遍认为，一系列精心设计的酶负责翻译后染色质标记，包括乙酰化和甲基化等，并且它们一起对基因调控产生深远影响。然而，情况并非总是如此。在这里，我们描述了 GCN5 最初鉴定为嗜热四膜虫的组蛋白乙酰转移酶的事件，以及它是酵母中转录共激活因子复合物的直系同源物的发现。