title: Bpur, the Lyme disease spirochete's PUR domain protein: identification as a transcriptional modulator and characterization of nucleic acid interactions.
abstract: The PUR domain is a nucleic acid-binding motif found in critical regulatory proteins of higher eukaryotes and in certain species of bacteria. During investigations into mechanisms by which the Lyme disease spirochete controls synthesis of its Erp surface proteins, it was discovered that the borrelial PUR domain protein, Bpur, binds with high affinity to double-stranded DNA adjacent to the erp transcriptional promoter. Bpur was found to enhance the effects of the erp repressor protein, BpaB. Bpur also bound single-stranded DNA and RNA, with relative affinities RNA > double-stranded DNA > single-stranded DNA. Rational site-directed mutagenesis of Bpur identified amino acid residues and domains critical for interactions with nucleic acids, and it revealed that the PUR domain has a distinct mechanism of interaction with each type of nucleic acid ligand. These data shed light on both gene regulation in the Lyme spirochete and functional mechanisms of the widely distributed PUR domain.
authors.affiliation: From the Department of Microbiology, Immunology, and Molecular Genetics and.
authors.forename: Brandon L
authors.initials: BL
authors.lastname: Jutras
authors.affiliation: From the Department of Microbiology, Immunology, and Molecular Genetics and.
authors.forename: Alicia M
authors.initials: AM
authors.lastname: Chenail
authors.affiliation: the Graduate Center for Toxicology, University of Kentucky College of Medicine, Lexington, Kentucky 40536.
authors.forename: Dustin W
authors.initials: DW
authors.lastname: Carroll
authors.affiliation: the James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202, and.
authors.forename: M Clarke
authors.initials: MC
authors.lastname: Miller
authors.affiliation: the Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, Kentucky 40536.
authors.forename: Haining
authors.initials: H
authors.lastname: Zhu
authors.affiliation: From the Department of Microbiology, Immunology, and Molecular Genetics and.
authors.forename: Amy
authors.initials: A
authors.lastname: Bowman
authors.affiliation: From the Department of Microbiology, Immunology, and Molecular Genetics and. Electronic address: brian.stevenson@uky.edu.
authors.forename: Brian
authors.initials: B
authors.lastname: Stevenson
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D025065:Borrelia burgdorferi / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008193:Lyme Disease / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics; D017434:Protein Structure, Tertiary; D012329:RNA, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D008565:Membrane Proteins; D012329:RNA, Bacterial; D016601:RNA-Binding Proteins
keywords: Bacteria; Borrelia burgdorferi; DNA-binding Protein; Gene Regulation; PUR Domain; RNA-binding Protein; Transcription Regulation; erp