STRUCTURE DETERMINATION OF EUKARYOTIC TRANSCRIPTION FACTOR TAF1 ALPHA

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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. The adenovirus (Ad) genome complexed with viral core proteins designated Ad core is the template for transcription of early genes and the first round of replication in Ad-infected cells. A cellular protein designated template-activating factor-I (TAF-I) is found to be involved in remodeling of the Ad core in vitro. We found that TAF-I interacts with the Ad DNA through core protein VII in infected cells in early phases of infection. In vitro binding assays using recombinant proteins showed that TAF-I forms ternary complexes with DNA¿¿¿¿¿"protein VII complexes. We crystallized the human TAF1 protein by the hanging-drop method. The crystal structure should shed light on the protein-protein interaction between virus and host, and give some idea of the drug design.