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.
Highlights
Borrelia burgdorferi controls protein production during its infectious cycle
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 doublestranded DNA adjacent to the erp transcriptional promoter
We present identification of the third erp operator-binding protein, Bpur, evaluation of its effects on erp expression, and characterization of mechanisms by which Bpur interacts with nucleic acids
Summary
Borrelia burgdorferi controls protein production during its infectious cycle. Results: Bpur was identified and shown to enhance effects of the erp transcriptional repressor, BpaB. 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 doublestranded DNA adjacent to the erp transcriptional promoter. 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. We present identification of the third erp operator-binding protein, Bpur (borrelial PUR domain protein), evaluation of its effects on erp expression, and characterization of mechanisms by which Bpur interacts with nucleic acids. PUR domain proteins are so-named because that motif binds
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