STRUCTURAL ANALYSIS OF THE RIBOSOMAL ENHANCESOME

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 在真核生物中，核糖体RNA基因的转录需要许多蛋白质的作用来启动和延长rRNA转录本。上游结合蛋白(UBF)是这一过程的关键调节因子。它不仅有助于核糖体RNA基因的激活，而且对稳定rRNA基因的DNA结构也很重要。已知UBF的前44 kDa是形成称为核糖体增强的核蛋白复合体所必需的。为了解释UBF参与RNA聚合酶I转录调控的广泛生化数据，了解UBF增强的原子分辨率结构是必不可少的。我们建议使用冷冻-EM和希望的X射线结晶学方法来确定该络合物的结构特征。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Transcription of ribosomal RNA genes in Eukaryotes requires the action of a number of proteins for initiation and elongation of rRNA transcripts. The Upstream Binding Protein (UBF) is a key regulator of this process. Not only does it facilitate the activation of the ribosomal RNA genes, but it is important for stabilizing the DNA structure of the rRNA genes. It is known that the first 44 kDa of UBF is required for formation of a nucleoprotein complex called the ribosomal enhancesome. In order to interpret the extensive biochemical data implicating UBF in regulation of RNA polymerase I transcription, it is essential to understand the structure of the UBF enhancesome at atomic resolution. We propose to determine the structural features of this complex using cryo-EM and hopefully X-ray crystallography methods.