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Andreas Bøggild

Crystal Structure of the VapBC Toxin–Antitoxin Complex from Shigella flexneri Reveals a Hetero-Octameric DNA-Binding Assembly

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  • Christian Dienemann, 1Centre for mRNP Biogenesis and Metabolism, Department of Molecular Biology and Genetics, Aarhus University, Denmark
  • Andreas Bøggild
  • Kristoffer S. Winther, 2Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, United Kingdom
  • Kenn Gerdes, 2Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, United Kingdom
  • Ditlev Brodersen
Toxin–antitoxin (TA) loci are common in archaea and prokaryotes and
allow cells to rapidly adapt to changing environmental conditions through
release of active regulators of metabolism. Many toxins are endonucleases
that target cellular mRNA and tRNAs, while the antitoxins tightly wrap
around the toxins to inhibit them under normal circumstances. The
antitoxins also bind to operators in the promoter regions of the cognate
TA operon and thereby regulate transcription. For enteric vapBC TA loci, the
VapC toxins specifically cleave tRNAfMet and thus down-regulate protein
synthesis. Here, we describe the crystal structure of the intact Shigella
flexneri VapBC TA complex, determined to 2.7 Å resolution. Both in solution
and in the crystal structure, four molecules of each protein combine to form
a large and globular hetero-octameric assembly with SpoVT/AbrB-type
DNA-binding domains at each end and a total molecular mass of about
100 kDa. The structure gives new insights into the inhibition of VapC toxins
by VapB and provides the molecular basis for understanding transcriptional
regulation through VapB dimerization.
Original languageEnglish
JournalJournal of Molecular Biology
Volume414
Issue5
Pages (from-to)713-722
Number of pages10
ISSN0022-2836
DOIs
Publication statusPublished - 16 Dec 2011

    Research areas

  • RNA interferase, tRNA, protein–DNA interaction

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