TY - JOUR
T1 - BpaB, a novel protein encoded by the Lyme disease spirochete's cp32 prophages, binds to erp Operator 2 DNA
AU - Burns, Logan H.
AU - Adams, Claire A.
AU - Riley, Sean P.
AU - Jutras, Brandon L.
AU - Bowman, Amy
AU - Chenail, Alicia M.
AU - Cooley, Anne E.
AU - Haselhorst, Laura A.
AU - Moore, Alisha M.
AU - Babb, Kelly
AU - Fried, Michael G.
AU - Stevenson, Brian
N1 - Funding Information:
Funding for open access charge: US National Institutes of Health (grant R01-AI044254 to B. S. and R01-GM070662 to M.F.); NIH Training Grant in Microbial Pathogenesis T32-AI49795 (to L.B. and S.R.).
PY - 2010/4/26
Y1 - 2010/4/26
N2 - Borrelia 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.
AB - Borrelia 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.
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U2 - 10.1093/nar/gkq284
DO - 10.1093/nar/gkq284
M3 - Article
C2 - 20421207
AN - SCOPUS:77956540768
SN - 0305-1048
VL - 38
SP - 5443
EP - 5455
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 16
M1 - gkq284
ER -