The Intrinsically Disordered Domain of the Antitoxin Phd Chaperones the Toxin Doc Against Irreversible Inactivation and Misfolding

Steven De Gieter, Albert Konijnenberg, Ariel Talavera Perez, Annika Butterer, Sarah Haesaerts, Henri De Greve, Frank Sobott, Remy Loris, Abel Garcia Pino

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

The toxin Doc from the phd/doc toxin-antitoxin module targets the cellular translation machinery and is inhibited by its antitoxin partner Phd. Here we show that Phd also functions as a chaperone, keeping Doc in an active, correctly folded conformation. In absence of Phd, Doc exists in a relatively expanded state that is prone to dimerization through domain swapping with its active site loop acting as hinge region. The domain-swapped dimer is not capable of arresting protein synthesis in vitro while the Doc monomer is. Upon binding to Phd, Doc becomes more compact and is secured in its monomeric state with a neutralized active site.
Original languageEnglish
Pages (from-to)34013-34023
Number of pages11
JournalJ. Biol. Chem.
Volume289
DOIs
Publication statusPublished - 2014

Keywords

  • Persistence
  • Structural biology
  • X-ray crystallography
  • Small Angle X-ray scatter
  • Protein folding
  • Protein misfolding
  • Toxin-antitoxin module
  • Bacterial stress response
  • Molecular biophysics

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