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BpaB, a novel protein encoded by the Lyme disease spirochete’s cp32 prophages, binds to erp Operator 2 DNA

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dc.contributor.authorBurns, Logan H.en
dc.contributor.authorAdams, Claire A.en
dc.contributor.authorRiley, Sean P.en
dc.contributor.authorJutras, Brandon L.en
dc.contributor.authorBowman, Amyen
dc.contributor.authorChenail, Alicia M.en
dc.contributor.authorCooley, Anne E.en
dc.contributor.authorHaselhorst, Laura A.en
dc.contributor.authorMoore, Alisha M.en
dc.contributor.authorBabb, Kellyen
dc.contributor.authorFried, Michael G.en
dc.contributor.authorStevenson, Brianen
dc.contributor.departmentBiochemistryen
dc.date.accessioned2019-02-13T14:12:50Zen
dc.date.available2019-02-13T14:12:50Zen
dc.date.issued2010en
dc.description.abstractBorrelia burgdorferi produces Erp outer surface proteins throughout mammalian infection, but represses their synthesis during colonization of vector ticks. A DNA region 50 of the start of erp transcription, Operator 2, was previously shown to be essential for regulation of expression. We now report identification and characterization of a novel erp Operator 2-binding protein, which we named BpaB. erp operons are located on episomal cp32 prophages, and a single bacterium may contain as many as 10 different cp32s. Each cp32 family member encodes a unique BpaB protein, yet the three tested cp32-encoded BpaB alleles all bound to the same DNA sequence. A 20-bp region of erp Operator 2 was determined to be essential for BpaB binding, and initial protein binding to that site was required for binding of additional BpaB molecules. A 36-residue region near the BpaB carboxy terminus was found to be essential for high-affinity DNA-binding. BpaB competed for binding to erp Operator 2 with a second B. burgdorferi DNAbinding protein, EbfC. Thus, cellular levels of free BpaB and EbfC could potentially control erp transcription levels.en
dc.description.sponsorshipUS National Institutes of Healthen
dc.description.sponsorshipNIH: R01-AI044254en
dc.description.sponsorshipNIH: R01-GM070662en
dc.description.sponsorshipNIH Training Grant in Microbial Pathogenesis T32-AI49795en
dc.identifier.doihttps://doi.org/10.1093/nar/gkq284en
dc.identifier.issue16en
dc.identifier.urihttp://hdl.handle.net/10919/87568en
dc.identifier.volume38en
dc.language.isoenen
dc.publisherOxford University Pressen
dc.rightsCreative Commons Attribution-NonCommercial 3.0 United Statesen
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/us/en
dc.titleBpaB, a novel protein encoded by the Lyme disease spirochete’s cp32 prophages, binds to erp Operator 2 DNAen
dc.title.serialNucleic Acids Researchen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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