Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
dc.contributor.author | Hyde, Eva I. | |
dc.contributor.author | Callow, Philip | |
dc.contributor.author | Rajasekar, Karthik V. | |
dc.contributor.author | Timmins, Peter | |
dc.contributor.author | Patel, Trushar R. | |
dc.contributor.author | Siligardi, Giuliano | |
dc.contributor.author | Hussain, Rohanah | |
dc.contributor.author | White, Scott A. | |
dc.contributor.author | Thomas, Christopher M. | |
dc.contributor.author | Scott, David J. | |
dc.date.accessioned | 2024-08-06T21:00:17Z | |
dc.date.available | 2024-08-06T21:00:17Z | |
dc.date.issued | 2017 | |
dc.description | Open access article. Creative Commons Attribution International license (CC BY 4.0) applies | |
dc.description.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. | |
dc.identifier.citation | Hyde, E. I., Callow, P., Rajasekar, K. V., Timmins, P., Patel, T. R., Siligardi, G., Hussain, R., White, S. A., Thomas, C. M., & Scott, D. J. (2017). Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA. Biochemical Journal, 473(18), 3121-3135. https://doi.org/10.1042/BCJ20170281 | |
dc.identifier.uri | https://hdl.handle.net/10133/6839 | |
dc.language.iso | en | |
dc.publisher | Portland Press | |
dc.publisher.department | Department of Chemistry and Biochemistry | |
dc.publisher.faculty | Arts and Science | |
dc.publisher.institution | University of Birmingham | |
dc.publisher.institution | Institut Laue Langevin | |
dc.publisher.institution | Harwell Science and Innovation Campus | |
dc.publisher.institution | University of Nottingham | |
dc.publisher.institution | Harwell Rutherford Appleton Laboratory | |
dc.publisher.institution | University of Lethbridge | |
dc.subject | Circular dichrosim | |
dc.subject | Intrinsically disordered proteins | |
dc.subject | Protein-DNA interactions | |
dc.subject | Protein-protein interactions | |
dc.subject | Small-angle scattering | |
dc.subject | Transcription regulation | |
dc.title | Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA | |
dc.type | Article |