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    A manganese-rich environment supports superoxide dismutase activity in a lyme disease pathogen, Borrelia burgdorferi

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    BbSodApaperFINAL.pdf (1.296Mb)
    Date
    2013-01-28
    Author
    Aguirre, J. Dafhne  Concept link
    Clark, Hillary M.  Concept link
    McIlvin, Matthew R.  Concept link
    Vazquez, Christine  Concept link
    Palmere, Shaina L.  Concept link
    Grab, Dennis J.  Concept link
    Seshu, J.  Concept link
    Hart, P. John  Concept link
    Saito, Mak A.  Concept link
    Culotta, Valeria C.  Concept link
    Metadata
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    Citable URI
    https://hdl.handle.net/1912/5836
    As published
    https://doi.org/10.1074/jbc.M112.433540
    Keyword
     Lyme disease; Manganese; Iron; Superoxide dismutase; Mitochondria 
    Abstract
    The Lyme disease pathogen Borrelia burgdorferi represents a novel organism in which to study metalloprotein biology in that this spirochete has uniquely evolved with no requirement for iron. Not only is iron low, but we show here that B. burgdorferi has the capacity to accumulate remarkably high levels of manganese. This high manganese is necessary to activate the SodA superoxide dismutase (SOD) essential for virulence. Using a metalloproteomic approach, we demonstrate that a bulk of B. burgdorferi SodA directly associates with manganese and a smaller pool of inactive enzyme accumulates as apoprotein. Other metalloproteins may have similarly adapted to using manganese as co-factor including the BB0366 amino-peptidase. While B. burgdorferi SodA has evolved in a manganese-rich, iron-poor environment, the opposite is true for Mn-SODs of organisms such as E. coli and bakers’ yeast. These Mn-SODs still capture manganese in an iron-rich cell, and we tested whether the same is true for Borrelia SodA. When expressed in the iron-rich mitochondria of S. cerevisiae, B. burgdorferi SodA was inactive. Activity was only possible when cells accumulated extremely high levels of manganese that exceeded cellular iron. Moreover, there was no evidence for iron inactivation of the SOD. B. burgdorferi SodA shows strong overall homology with other members of the Mn-SOD family, but computer assisted modeling revealed some unusual features of the hydrogen bonding network near the enzyme’s active site. The unique properties of B. burgdorferi SodA may represent adaptation to expression in the manganese-rich and iron-poor environment of the spirochete.
    Description
    Author Posting. © The Author(s), 2013. This is the author's version of the work. It is posted here by permission of American Society for Biochemistry and Molecular Biology for personal use, not for redistribution. The definitive version was published in Journal of Biological Chemistry 288 (2013): 8468-8478, doi:10.1074/jbc.M112.433540.
    Collections
    • Marine Chemistry and Geochemistry (MC&G)
    Suggested Citation
    Preprint: Aguirre, J. Dafhne, Clark, Hillary M., McIlvin, Matthew R., Vazquez, Christine, Palmere, Shaina L., Grab, Dennis J., Seshu, J., Hart, P. John, Saito, Mak A., Culotta, Valeria C., "A manganese-rich environment supports superoxide dismutase activity in a lyme disease pathogen, Borrelia burgdorferi", 2013-01-28, https://doi.org/10.1074/jbc.M112.433540, https://hdl.handle.net/1912/5836
     

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