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Physiology

Insights into the Function of the N-Acetyltransferase SatA That Detoxifies Streptothricin in Bacillus subtilis and Bacillus anthracis

Rachel M. Burckhardt, Jorge C. Escalante-Semerena
Marie A. Elliot, Editor
Rachel M. Burckhardt
aDepartment of Microbiology, University of Georgia, Athens, Georgia, USA
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Jorge C. Escalante-Semerena
aDepartment of Microbiology, University of Georgia, Athens, Georgia, USA
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Marie A. Elliot
McMaster University
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DOI: 10.1128/AEM.03029-18
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ABSTRACT

Acylation of epsilon amino groups of lysyl side chains is a widespread modification of proteins and small molecules in cells of all three domains of life. Recently, we showed that Bacillus subtilis and Bacillus anthracis encode the GCN5-related N-acetyltransferase (GNAT) SatA that can acetylate and inactivate streptothricin, which is a broad-spectrum antibiotic produced by actinomycetes in the soil. To determine functionally relevant residues of B. subtilis SatA (BsSatA), a mutational screen was performed, highlighting the importance of a conserved area near the C terminus. Upon inspection of the crystal structure of the B. anthracis Ames SatA (BaSatA; PDB entry 3PP9), this area appears to form a pocket with multiple conserved aromatic residues; we hypothesized this region contains the streptothricin-binding site. Chemical and site-directed mutagenesis was used to introduce missense mutations into satA, and the functionality of the variants was assessed using a heterologous host (Salmonella enterica). Results of isothermal titration calorimetry experiments showed that residue Y164 of BaSatA was important for binding streptothricin. Results of size exclusion chromatography analyses showed that residue D160 was important for dimerization. Together, these data advance our understanding of how SatA interacts with streptothricin.

IMPORTANCE This work provides insights into how an abundant antibiotic found in soil is bound to the enzyme that inactivates it. This work identifies residues for the binding of the antibiotic and probes the contributions of substituting side chains for those in the native protein, providing information regarding hydrophobicity, size, and flexibility of the antibiotic binding site.

FOOTNOTES

    • Received 17 December 2018.
    • Accepted 9 January 2019.
    • Accepted manuscript posted online 18 January 2019.
  • Supplemental material for this article may be found at https://doi.org/10.1128/AEM.03029-18.

  • Copyright © 2019 American Society for Microbiology.

All Rights Reserved.

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Insights into the Function of the N-Acetyltransferase SatA That Detoxifies Streptothricin in Bacillus subtilis and Bacillus anthracis
Rachel M. Burckhardt, Jorge C. Escalante-Semerena
Applied and Environmental Microbiology Mar 2019, 85 (6) e03029-18; DOI: 10.1128/AEM.03029-18

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Insights into the Function of the N-Acetyltransferase SatA That Detoxifies Streptothricin in Bacillus subtilis and Bacillus anthracis
Rachel M. Burckhardt, Jorge C. Escalante-Semerena
Applied and Environmental Microbiology Mar 2019, 85 (6) e03029-18; DOI: 10.1128/AEM.03029-18
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KEYWORDS

Bacillus anthracis
Bacillus subtilis
N-acetyltransferases
streptothricin
antibiotic resistance

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