STRUCTURAL STUDIES OF DNA RECOMBINASES AND INDIRECT RECOGNITION OF DNA SEQUENCE

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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. Structural studies of DNA recognition & recombination Our research focuses on the structural understanding of DNA recombination reactions. For several of the enzymes we study (Rad51, Flp, and Sin) we have determined initial structures and are now working towards a deeper understanding of their mechanism through additional structural and biochemical studies. For example, for the serine recombinase Sin, we hope to determine the structures of the protein bound to different binding sites and of the large multi-protein complex within which the enzyme normally functions. For another project, the transposase from phage mu, we have crystals of the final transposition complex (4 ~60kDa protomers plus 135bp of DNA) that diffract to modest resolution, but we need more and better data to solve the phase problem. This would be the first structure of a product complex for any DNA transposase. Finally, we are also studying the interactions of the E. coli SOS response regulator LexA with DNA.