STRUCTURAL ANALYSIS OF THE RIBOSOMAL ENHANCESOME

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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.