The Borrelia burgdorferi BpaB proteins of the spirochete's ubiquitous cp32 prophages are DNA-binding proteins, required both for maintenance of the bacteriophage episomes and for transcriptional regulation of the cp32 erp operons. Through use of DNase I footprinting, we demonstrate that BpaB binds the erp operator initially at the sequence 5′-TTATA-3′. Electrophoretic mobility shift assays indicated that BpaB also binds with high affinity to sites located in the 5′ noncoding regions of two additional cp32 genes. Characterization of the proteins encoded by those genes indicated that they are a single-stranded DNA-binding protein and a nuclease, which we named SsbP and NucP, respectively. Chromatin immunoprecipitation indicated that BpaB binds erp, ssbP, and nucP in live B. burgdorferi. A mutant bacterium that overexpressed BpaB produced significantly higher levels of ssbP and nucP transcript than did the wild-type parent.

Document Type


Publication Date


Notes/Citation Information

Published in Journal of Bacteriology, v. 194, no. 17, p. 4570-4578.

Copyright © 2012, American Society for Microbiology. All Rights Reserved.

The copyright holder has granted the permission for posting the article here.

A correction to this article can be found at https://doi.org/10.1128/JB.00661-12.

Digital Object Identifier (DOI)


Funding Information

This work was funded by National Institutes of Health grant R01-AI044254 to Brian Stevenson.