title: A biochemical characterization of the DNA binding activity of the response regulator VicR from Streptococcus mutans.
abstract: Two-component systems (TCSs) are ubiquitous among bacteria and are among the most elegant and effective sensing systems in nature. They allow for efficient adaptive responses to rapidly changing environmental conditions. In this study, we investigated the biochemical characteristics of the Streptococcus mutans protein VicR, an essential response regulator that is part of the VicRK TCS. We dissected the DNA binding requirements of the recognition sequences for VicR in its phosphorylated and unphosphorylated forms. In doing so, we were able to make predictions for the expansion of the VicR regulon within S. mutans. With the ever increasing number of bacteria that are rapidly becoming resistant to even the antibiotics of last resort, TCSs such as the VicRK provide promising targets for a new class of antimicrobials.
authors.affiliation: Department of Molecular and Computational Biology, Division of Biomedical Science, Herman Ostrow School of Dentistry, The University of Southern California, Los Angeles, California, United States of America.
authors.forename: Eduardo
authors.initials: E
authors.lastname: Ayala
authors.affiliation: Department of Molecular and Computational Biology, Division of Biomedical Science, Herman Ostrow School of Dentistry, The University of Southern California, Los Angeles, California, United States of America.
authors.forename: Jennifer S
authors.initials: JS
authors.lastname: Downey
authors.affiliation: Center for Microbial Pathogenesis, The Research Institute, Nationwide Children's Hospital, Columbus, Ohio, United States of America.
authors.forename: Lauren
authors.initials: L
authors.lastname: Mashburn-Warren
authors.affiliation: Dental Research Institute, Faculty of Dentistry, University of Toronto, Toronto, Canada.
authors.forename: Dilani B
authors.initials: DB
authors.lastname: Senadheera
authors.affiliation: Dental Research Institute, Faculty of Dentistry, University of Toronto, Toronto, Canada.
authors.forename: Dennis G
authors.initials: DG
authors.lastname: Cvitkovitch
authors.affiliation: Department of Molecular and Computational Biology, Division of Biomedical Science, Herman Ostrow School of Dentistry, The University of Southern California, Los Angeles, California, United States of America; Center for Microbial Pathogenesis, The Research Institute, Nationwide Children's Hospital, Columbus, Ohio, United States of America.
authors.forename: Steven D
authors.initials: SD
authors.lastname: Goodman
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D016384:Consensus Sequence; D004247:DNA / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009154:Mutation; D010766:Phosphorylation; D011485:Protein Binding; D018085:Regulon / Q000235:genetics; D013295:Streptococcus mutans
chemical_list: D001426:Bacterial Proteins; C119939:YycF protein, Bacteria; D004247:DNA