Burns, Logan H.Adams, Claire A.Riley, Sean P.Jutras, Brandon L.Bowman, AmyChenail, Alicia M.Cooley, Anne E.Haselhorst, Laura A.Moore, Alisha M.Babb, KellyFried, Michael G.Stevenson, Brian2019-02-132019-02-132010http://hdl.handle.net/10919/87568Borrelia 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.enCreative Commons Attribution-NonCommercial 3.0 United StatesArticle - Refereedhttps://doi.org/10.1093/nar/gkq2843816