Jutras, Brandon L.Chenail, Alicia M.Rowland, Christi L.Carroll, Dustin W.Miller, M. ClarkeBykowski, TomaszStevenson, Brian2019-02-132019-02-132013-06-20http://hdl.handle.net/10919/87574A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG orthologues indicated that the Staphylococcus aureus protein also binds DNA, but interacts preferentially with a distinct nucleic acid sequence. Site-directed mutagenesis and domain swapping between the S. aureus and B. burgdorferi proteins identified that a 6-residue stretch of the SpoVG a-helix contributes to DNA sequence specificity. Two additional, highly conserved amino acid residues on an adjacent b-sheet are essential for DNA-binding, apparently by contacts with the DNA phosphate backbone. Results of these studies thus identified a novel family of bacterial DNA-binding proteins, developed a model of SpoVG-DNA interactions, and provide direction for future functional studies on these wide-spread proteins.application/pdfenCreative Commons Attribution 3.0 United StatesArticle - Refereedhttps://doi.org/10.1371/journal.pone.006668386