Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA

Eva Hyde, Phillip Callow, Karthik Rajasekar, Peter Timmins, Trushar Patel, Giuliano Siligardi, Rohanah Hussain, Scott White, Christopher Thomas, David Scott

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4 Citations (Scopus)
98 Downloads (Pure)

Abstract

The ParB protein, KorB, from the RK2 plasmid is required for DNA partitioning and
transcriptional repression. It acts co-operatively with other proteins, including the repressor KorA. Like many multifunctional proteins, KorB contains regions of intrinsically disordered structure, existing in a large ensemble of interconverting conformations. Using NMR spectroscopy, circular dichroism and small-angle neutron scattering, we studied KorB selectively within its binary complexes with KorA and DNA, and within the ternary KorA/KorB/DNA complex. The bound KorB protein remains disordered with a mobile C-terminal domain and no changes in the secondary structure, but increases in the radius of gyration on complex formation. Comparison of wild-type KorB with an N-terminal deletion mutant allows a model of the ensemble average distances between the domains when bound to DNA. We propose that the positive co-operativity between KorB, KorA and DNA results from conformational restriction of KorB on binding each partner, while maintaining disorder.
Original languageEnglish
Pages (from-to)3121–3135
Number of pages15
JournalBiochemical Journal
Volume474
Issue number18
Early online date31 Jul 2017
DOIs
Publication statusPublished - 31 Aug 2017

Keywords

  • small-angle scattering
  • transcription regulation
  • circular dichroism
  • intrinsically disordered proteins
  • protein–DNA interactions
  • protein–protein interactions

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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