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

dc.contributor.authorHyde, Eva I.
dc.contributor.authorCallow, Philip
dc.contributor.authorRajasekar, Karthik V.
dc.contributor.authorTimmins, Peter
dc.contributor.authorPatel, Trushar R.
dc.contributor.authorSiligardi, Giuliano
dc.contributor.authorHussain, Rohanah
dc.contributor.authorWhite, Scott A.
dc.contributor.authorThomas, Christopher M.
dc.contributor.authorScott, David J.
dc.date.accessioned2024-08-06T21:00:17Z
dc.date.available2024-08-06T21:00:17Z
dc.date.issued2017
dc.descriptionOpen access article. Creative Commons Attribution International license (CC BY 4.0) applies
dc.description.abstractThe 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.citationHyde, 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.urihttps://hdl.handle.net/10133/6839
dc.language.isoen
dc.publisherPortland Press
dc.publisher.departmentDepartment of Chemistry and Biochemistry
dc.publisher.facultyArts and Science
dc.publisher.institutionUniversity of Birmingham
dc.publisher.institutionInstitut Laue Langevin
dc.publisher.institutionHarwell Science and Innovation Campus
dc.publisher.institutionUniversity of Nottingham
dc.publisher.institutionHarwell Rutherford Appleton Laboratory
dc.publisher.institutionUniversity of Lethbridge
dc.subjectCircular dichrosim
dc.subjectIntrinsically disordered proteins
dc.subjectProtein-DNA interactions
dc.subjectProtein-protein interactions
dc.subjectSmall-angle scattering
dc.subjectTranscription regulation
dc.titleIntrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
dc.typeArticle
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