STRUCTURAL ANALYSIS OF THE RIBOSOMAL ENHANCESOME

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 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起始和延伸rRNA转录物。 上游结合蛋白（UBF）是这一过程的关键调节因子。 它不仅促进核糖体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体的核蛋白复合物所需的。 为了解释大量的生化数据暗示UBF在RNA聚合酶I转录的调节，它是必不可少的，以了解原子分辨率的UBF增强体的结构。我们建议使用cryo-EM和希望的X射线晶体学方法来确定这种复杂的结构特征。

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.