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Microbiology 142 (1996), 2471-2479; DOI  10.1099/00221287-142-9-2471
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Isolation of Borrelia burgdorferi genes encoding homologues of DNA-binding protein HU and ribosomal protein S20

Kit Tilly1,3, John Fuhrman1, Jim Campbell1 and D. Scott Samuels2,{dagger}

Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840, USA
Microscopy Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840, USA

3Author for correspondence: Kit Tilly. Tel: +1 406 363 9239. Fax: +1 406 363 9204. e-mail: ktilly@nih.gov

ABSTRACT

Linear DNA with covalently closed ends is the predominant form of DNA in the spirochaete Borrelia burgdorferi. All bacteria examined to date have small DNA-binding proteins related to the Escherichia coli IHF and HU proteins that appear to play roles in DNA compaction and replication, but such proteins had not been isolated from bacteria with linear genomes. We found a single gene in B. burgdorferi (named hbb) whose product (named Hbb) complements the defects for {gamma} DNA packaging found in E. coli strains mutant in the genes for IHF and HU. The sequence of the predicted B. burgdorferi protein is similar to those of HU and IHF-like proteins in other bacteria. The gene appears to be in an operon with the order rpsT-hbb-orfH, where the rpsT gene is a homologue of the E. coli gene encoding ribosomal protein S20 and the orfH gene encodes a protein of unknown function. This operon is located upstream of the previously identified B. burgdorferi rho homologue.


Keywords: Lyme disease, Borrelia burgdorferi, integration host factor (IHF), HU protein

{dagger} Present address: Division of Biological Sciences, University of Montana, Missoula, MT 59812, USA.




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