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Publication Abstract from PubMed

Toxin-antitoxin (TA) systems play critical roles in the environment adaptation of bacteria. Allosteric coupling between the N-terminal DNA-binding domain and the C-terminal toxin-binding domain of antitoxins contributes to conditional cooperativity in the functioning of type II TA. Herein, using circular dichroism (CD), nuclear magnetic resonance (NMR), X-ray crystallography, and size exclusion chromatography (SEC), the structure and DNA binding of CopASO, a newly identified type II antitoxin in Shewanella oneidensis, were investigated. Our data show that CopASO is a typical RHH antitoxin with an ordered N-terminal domain and a disordered C-terminal domain, and furthermore indicate that the C-terminal domain facilitates DNA binding of the N-terminal domain, which in turn induces the C-terminal domain to fold and associate.

Structure and allosteric coupling of type antitoxin CopASO.,Zhao R, Li Q, Zhang J, Li F, Yao J, Zhang J, Liu L, Wang X, Zhang X Biochem Biophys Res Commun. 2019 Jul 5;514(4):1122-1127. doi:, 10.1016/j.bbrc.2019.05.049. Epub 2019 May 14. PMID:31101334^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.