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B23-Circular Dichroism	Intrinsic disorder in the partitioning protein KorB persists after cooperative complex formation with operator DNA and KorA Eva Hyde , Phillip Callow , Karthik V. Rajasekar , Peter Timmins , Trushar R. Patel , Giuliano Siligardi , Rohanah Hussain , Scott White , Christopher M. Thomas , David J. Scott Biochemical Journal DOI: 10.1042/BCJ20170281 Diamond Proposal Number(s): [14894, 16440] Open Access Show Abstract ▼ 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 have 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 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.	Jul 2017

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B23-Circular Dichroism

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

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

Biochemical Journal

DOI: 10.1042/BCJ20170281

Diamond Proposal Number(s): [14894, 16440]