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The Lyme disease spirochete's BpuR DNA/RNA-binding protein is differentially expressed during the mammal-tick infectious cycle, which affects translation of the SodA superoxide dismutase.

Authors
  • Jutras, Brandon L1
  • Savage, Christina R1
  • Arnold, William K1
  • Lethbridge, Kathryn G1
  • Carroll, Dustin W2
  • Tilly, Kit3
  • Bestor, Aaron3
  • Zhu, Haining2
  • Seshu, Janakiram4
  • Zückert, Wolfram R5
  • Stewart, Philip E3
  • Rosa, Patricia A3
  • Brissette, Catherine A6
  • Stevenson, Brian1, 7
  • 1 Department of Microbiology, Immunology and Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY, USA.
  • 2 Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY, USA.
  • 3 Laboratory of Bacteriology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, USA.
  • 4 Department of Biology, University of Texas at San Antonio, San Antonio, TX, USA.
  • 5 Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, KS, USA.
  • 6 Department of Biomedical Sciences, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND, USA.
  • 7 Department of Entomology, University of Kentucky, Lexington, KY, USA.
Type
Published Article
Journal
Molecular Microbiology
Publisher
Wiley (Blackwell Publishing)
Publication Date
Sep 01, 2019
Volume
112
Issue
3
Pages
973–991
Identifiers
DOI: 10.1111/mmi.14336
PMID: 31240776
Source
Medline
Language
English
License
Unknown

Abstract

When the Lyme disease spirochete, Borrelia burgdorferi, transfers from a feeding tick into a human or other vertebrate host, the bacterium produces vertebrate-specific proteins and represses factors needed for arthropod colonization. Previous studies determined that the B. burgdorferi BpuR protein binds to its own mRNA and autoregulates its translation, and also serves as co-repressor of erp transcription. Here, we demonstrate that B. burgdorferi controls transcription of bpuR, expressing high levels of bpuR during tick colonization but significantly less during mammalian infection. The master regulator of chromosomal replication, DnaA, was found to bind specifically to a DNA sequence that overlaps the bpuR promoter. Cultured B. burgdorferi that were genetically manipulated to produce elevated levels of BpuR exhibited altered levels of several proteins, although BpuR did not impact mRNA levels. Among these was the SodA superoxide dismutase, which is essential for mammalian infection. BpuR bound to sodA mRNA in live B. burgdorferi, and a specific BpuR-binding site was mapped 5' of the sodA open reading frame. Recognition of posttranscriptional regulation of protein levels by BpuR adds another layer to our understanding of the B. burgdorferi regulome, and provides further evidence that bacterial protein levels do not always correlate directly with mRNA levels. © 2019 The Authors. Molecular Microbiology Published by John Wiley & Sons Ltd.

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