This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.One focus of the Brennan laboratory is on protein-nucleic acid interactions. We have entered into a collaboration to perform structural studies of the bacterial DNA binding protein FitA, and its dimerization partner, FitB, alone and when bound to DNA. The FitAB complex is interesting because it is implicated in the slow transit of Neisseria gonorrhoeae across epithelial monolayers, which is thought to be important for the development of asymptomatic carriers who spread gonococcal disease. When FitB is expressed alone, cells fail to divide properly, and we have hypothesized that FitA prevents FitB from interfering with the cellular machinery. The structure of the FitAB complex will provide (1) a representative of a class of proteins which are found on virulence plasmids and interfere with cell division (FitB) and (2) a ribbon-helix-helix DNA binding domain (FitA). The DNA-bound structure will show how the short beta strand at the amino terminus of FitA mediates specific interactions with a large segment of DNA.
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