Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorATools Hyde, Eva I., Callow, Phillip, Rajasekar, Karthik V., timmins, Peter, Patel, Trushar Patel, Siligardi, Giuliano, Hussain, Rohanah, White, Scott A., Thomas, Christopher M. and Scott, David J. (2017) Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA. Biochemical Journal, 474 (18). pp. 3121-3135. ISSN 0264-6021 Full text not available from this repository.
Official URL: http://www.biochemj.org/content/474/18/3121
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 betweenthe 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.
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