title: Topology of the Bacillus subtilis SpoIISA protein and its role in toxin-antitoxin function.
abstract: SpoIISAB is a toxin-antitoxin module encoded on the chromosomes of Bacillus subtilis and related Bacilli species. The SpoIISA toxin was previously shown to target the cytoplasmic membrane and to induce lysis in both B. subtilis and Escherichia coli; however, the precise manner of SpoIISA toxicity remains unknown. In this work, we focused on the N-terminal, transmembrane domain of SpoIISA and verified the prediction of its topology. Using truncated SpoIISA constructs, we show that the entire transmembrane domain is required for its toxicity. Moreover, we propose that the oligomerization of this transmembrane domain is crucial for activity of SpoIISA, possibly by forming a pore-like structure.
authors.affiliation: Institute of Molecular Biology, Slovak Academy of Sciences, Bratislava, Slovakia.
authors.forename: Jana
authors.initials: J
authors.lastname: Makroczyová
authors.forename: Stanislava
authors.initials: S
authors.lastname: Rešetárová
authors.forename: Patrik
authors.initials: P
authors.lastname: Florek
authors.forename: Imrich
authors.initials: I
authors.lastname: Barák
mesh_terms: D001412:Bacillus subtilis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001427:Bacterial Toxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology; D050296:Microbial Viability / Q000187:drug effects; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; C030069:spore-specific proteins, Bacillus
keywords: Bacillus subtilis; protein topology; toxin-antitoxin system