期刊
NUCLEIC ACIDS RESEARCH
卷 37, 期 6, 页码 1973-1983出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkp027
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资金
- US National Institutes of Health [R01-AI044254, R01-GM070662]
- National Institutes of Health [T32-AI49795]
- University of Kentucky
The Lyme disease spirochete, Borrelia burgdorferi, encodes a novel type of DNA-binding protein named EbfC. Orthologs of EbfC are encoded by a wide range of bacterial species, so characterization of the borrelial protein has implications that span the eubacterial kingdom. The present work defines the DNA sequence required for high-affinity binding by EbfC to be the 4 bp broken palindrome GTnAC, where n can be any nucleotide. Two high-affinity EbfC-binding sites are located immediately 5 of B. burgdorferi erp transcriptional promoters, and binding of EbfC was found to alter the conformation of erp promoter DNA. Consensus EbfC-binding sites are abundantly distributed throughout the B. burgdorferi genome, occurring approximately once every 1 kb. These and other features of EbfC suggest that this small protein and its orthologs may represent a distinctive type of bacterial nucleoid-associated protein. EbfC was shown to bind DNA as a homodimer, and site-directed mutagenesis studies indicated that EbfC and its orthologs appear to bind DNA via a novel -helical tweezer-like structure.
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