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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.
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 language | English |
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Pages (from-to) | 3121–3135 |
Number of pages | 15 |
Journal | Biochemical Journal |
Volume | 474 |
Issue number | 18 |
Early online date | 31 Jul 2017 |
DOIs | |
Publication status | Published - 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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Dive into the research topics of 'Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA'. Together they form a unique fingerprint.Projects
- 1 Finished
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HWB:NMR: a national resource for biomolecular research
Overduin, M., Guenther, U., Ludwig, C., Arvanitis, T., Dafforn, T., Hyde, E., Levine, B., Peet, A. & Viant, M.
1/12/12 → 28/02/18
Project: Research