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- W2090782442 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." @default.
- W2090782442 created "2016-06-24" @default.
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- W2090782442 date "2013-09-01" @default.
- W2090782442 modified "2023-10-12" @default.
- W2090782442 title "Bpur, the Lyme Disease Spirochete's PUR Domain Protein" @default.
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- W2090782442 doi "https://doi.org/10.1074/jbc.m113.491357" @default.
- W2090782442 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3764826" @default.
- W2090782442 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23846702" @default.
- W2090782442 hasPublicationYear "2013" @default.
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