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. Author manuscript; available in PMC: 2017 May 3.
Published in final edited form as: Biochemistry. 2016 Apr 15;55(17):2510–2517. doi: 10.1021/acs.biochem.6b00083

Figure 1.

Figure 1

Mutagenesis does not affect SMase activity but inhibits the ability of β-toxin to oligomerize. (a) Amino acid sequence of β-toxin. Highlighted areas are regions predicted to be biologically important by Huseby et al.2, 14 Black asterisks denote residues mutated, those in white indicate changes that disrupted the DNA biofilm ligase activity. Gray asterisk indicates residue mutated to disrupt SMase activity. (b) All DNA biofilm ligase mutants retain ability to lyse sheep blood erythrocytes similar to wild type as seen by zones of lysis surrounding growth on sheep blood agar plates. (c) DNA precipitation assays performed with β-toxin recovered from expression in S. aureus RN450Δhlb nuc-. Mutants T149a, H162A, and D163A were unable to form precipitates at up to 200 μg of β-toxin. Wild type and mutant T151A formed a precipitate beginning at 50 μg of protein, and C158A at 60 μg.