Borrelia burgdorferi SpoVG DNA-and RNA-binding protein modulates the physiology of the Lyme disease spirochete

CR Savage, BL Jutras, A Bestor, K Tilly… - Journal of …, 2018 - Am Soc Microbiol
CR Savage, BL Jutras, A Bestor, K Tilly, PA Rosa, Y Tourand, PE Stewart, CA Brissette
Journal of Bacteriology, 2018Am Soc Microbiol
ABSTRACT The SpoVG protein of Borrelia burgdorferi, the Lyme disease spirochete, binds
to specific sites of DNA and RNA. The bacterium regulates transcription of spoVG during the
natural tick-mammal infectious cycle and in response to some changes in culture conditions.
Bacterial levels of spoVG mRNA and SpoVG protein did not necessarily correlate,
suggesting that posttranscriptional mechanisms also control protein levels. Consistent with
this, SpoVG binds to its own mRNA, adjacent to the ribosome-binding site. SpoVG also …
Abstract
The SpoVG protein of Borrelia burgdorferi, the Lyme disease spirochete, binds to specific sites of DNA and RNA. The bacterium regulates transcription of spoVG during the natural tick-mammal infectious cycle and in response to some changes in culture conditions. Bacterial levels of spoVG mRNA and SpoVG protein did not necessarily correlate, suggesting that posttranscriptional mechanisms also control protein levels. Consistent with this, SpoVG binds to its own mRNA, adjacent to the ribosome-binding site. SpoVG also binds to two DNA sites in the glpFKD operon and to two RNA sites in glpFKD mRNA; that operon encodes genes necessary for glycerol catabolism and is important for colonization in ticks. In addition, spirochetes engineered to dysregulate spoVG exhibited physiological alterations.
IMPORTANCE B. burgdorferi persists in nature by cycling between ticks and vertebrates. Little is known about how the bacterium senses and adapts to each niche of the cycle. The present studies indicate that B. burgdorferi controls production of SpoVG and that this protein binds to specific sites of DNA and RNA in the genome and transcriptome, respectively. Altered expression of spoVG exerts effects on bacterial replication and other aspects of the spirochete's physiology.
American Society for Microbiology