The overall goal is to provide a structural basis for understanding the mechanisms of initiation and elongation by DNA and RNA polymerases, their transitions from initiation to elongation phases, the regulation of polymerases by factors and the mechanisms by which these polymerases assure that the correct nucleotide is inserted. This objective will be achieved by determining the crystal structures of polymerases complexed with functionally associated proteins and bound to appropriate DNA or RNA substrates, as well as by appropriate biochemical experiments.
We aim to establish the structures of component assemblies of the replisome. These include a replication fork complex with DNA polymerase III, tau and a forked-DNA substrate, as well as the structure of the primasome that includes Thermus aquaticus DNAB helicase complexed with the DNAG primase bound to their DNA substrate. Additionally, the structure of the DNAB helicase bound to its DNA and nucleotide substrates as well as that of the clamp loading protein bound to its DNA substrate, sliding clamp and single-stranded DNA binding protein will be established. The structural basis of the initiation of DNA synthesis by the protein primed
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