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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Structural insight into the E. coli HigBA complex.

Jingsi Yang1, Ke Zhou2, Peng Liu2

  • 1School of Life Sciences, University of Dalian Science and Technology, Dalian, Liaolin Province, 230027, People's Republic of China.

Biochemical and Biophysical Research Communications
|September 8, 2016
PubMed
Summary

Bacterial toxin-antitoxin systems regulate cell fitness. Researchers solved the HigBA complex structure, revealing how the antitoxin HigA binds the toxin HigB and DNA, crucial for bacterial survival.

Keywords:
HigBAToxin-antitoxin

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Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • Toxin-antitoxin systems are widespread in bacteria and archaea, influencing cell fitness in response to environmental changes.
  • These systems play roles in various cellular processes, including stress response and plasmid maintenance.

Purpose of the Study:

  • To determine the crystal structure of the Escherichia coli K-12 HigBA toxin-antitoxin complex.
  • To elucidate the structural basis of the interaction between the HigB toxin and the HigA antitoxin.
  • To investigate the role of HigA in DNA binding and complex formation.

Main Methods:

  • X-ray crystallography was used to solve the structure of the HigBA complex at 2.7 Å resolution.
  • Biochemical assays were performed to assess DNA-binding capabilities of different complex forms.
  • Structural analysis focused on the subunit interactions and domain functions.

Main Results:

  • The HigBA complex forms a hetero-tetramer ((HigBA)2) composed of two HigB and two HigA subunits.
  • The toxin HigB adopts an RNase T1 fold, while the antitoxin HigA forms a C-shaped clamp around HigB.
  • HigA dimerization via its N-terminal domain is essential for tetramer formation but not for DNA binding; the C-terminal domain with a helix-turn-helix motif is crucial for DNA binding.
  • The HigBA complex binds specifically to two palindromic sequences within the higBA operator DNA in vitro.

Conclusions:

  • The crystal structure reveals the molecular architecture of the E. coli HigBA toxin-antitoxin complex.
  • HigA's dimerization and its C-terminal DNA-binding domain are key for regulating the toxin-antitoxin system's function.
  • Understanding the HigBA structure provides insights into bacterial gene regulation and survival mechanisms.