PDF(Pubmed)
Abstract：
The NuA3 complex is a major regulator of gene transcription and the cell cycle in yeast. Five core subunits are required for complex assembly and function, but it remains unclear how these subunits interact to form the complex. Here, we report that the Taf14 subunit of the NuA3 complex binds to two other subunits of the complex, Yng1 and Sas3, and describe the molecular mechanism by which the extra-terminal domain of Taf14 recognizes the conserved motif present in Yng1 and Sas3. Structural, biochemical, and mutational analyses show that two motifs are sandwiched between the two extra-terminal domains of Taf14. The head-to-toe dimeric complex enhances the DNA binding activity of Taf14, and the formation of the hetero-dimer involving the motifs of Yng1 and Sas3 is driven by sequence complementarity. In vivo assays in yeast demonstrate that the interactions of Taf14 with both Sas3 and Yng1 are required for proper function of the NuA3 complex in gene transcription and DNA repair. Our findings suggest a potential basis for the assembly of three core subunits of the NuA3 complex, Taf14, Yng1 and Sas3.
摘要：
NuA3复合物是酵母中基因转录和细胞周期的主要调控因子。复杂的组装和功能需要五个核心子单元，但目前尚不清楚这些亚基是如何相互作用形成复合体的。这里,我们报道了NuA3复合物的Taf14亚基与复合物的另外两个亚基结合，Yng1和Sas3，并描述了Taf14的末端外结构域识别存在于Yng1和Sas3中的保守基序的分子机制。结构,生物化学，和突变分析表明，两个基序夹在Taf14的两个外末端结构域之间。从头到脚的二聚体复合物增强了Taf14的DNA结合活性，并且涉及Yng1和Sas3基序的异源二聚体的形成是由序列互补性驱动的。酵母中的体内测定表明，Taf14与Sas3和Yng1的相互作用对于NuA3复合物在基因转录和DNA修复中的正常功能是必需的。我们的研究结果表明了NuA3复合物的三个核心亚基组装的潜在基础，Taf14、Yng1和Sas3。
