Structure and allosteric coupling of type Ⅱ antitoxin CopASO

Biochem Biophys Res Commun. 2019 Jul 5;514(4):1122-1127. doi: 10.1016/j.bbrc.2019.05.049. Epub 2019 May 14.

Abstract

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.

Keywords: Allosteric coupling; Antitoxin; CopA(SO); Ribbon-helix-helix motif; Shewanella oneidensis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Antitoxins / chemistry*
  • Antitoxins / metabolism*
  • Circular Dichroism
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA / metabolism
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Shewanella / chemistry*

Substances

  • Antitoxins
  • DNA

Supplementary concepts

  • Shewanella oneidensis