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

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

Authors

Phillip Callow

Eva I. Hyde

Karthik V. Rajasekar

Trushar Patel Patel

Peter Timmins

Giuliano Siligardi

Rohanah Hussain

Scott A. White

Christopher M. Thomas

David J. Scott



Abstract

© 2017 The Author(s). 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.

Journal Article Type Article
Publication Date Aug 31, 2017
Journal Biochemical Journal
Print ISSN 0264-6021
Electronic ISSN 1470-8728
Publisher Portland Press
Peer Reviewed Peer Reviewed
Volume 474
Issue 18
Pages 3121-3135
APA6 Citation Hyde, E. I., Callow, P., Rajasekar, K. V., Timmins, P., Patel, T. P., Siligardi, G., …Scott, D. J. (2017). Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA. Biochemical Journal, 474(18), 3121-3135. https://doi.org/10.1042/BCJ20170281
DOI https://doi.org/10.1042/BCJ20170281
Keywords Cell Biology; Biochemistry; Molecular Biology
Publisher URL http://www.biochemj.org/content/474/18/3121
Copyright Statement Copyright information regarding this work can be found at the following address: http://creativecommons.org/licenses/by/4.0
Additional Information This work is based in 10 years of data acquisition that started in 2007 at the ILL in Grenoble. Data was acquired at the ILL and ISIS (Oxfordshire) neutron sources, with circular dichroism data obtained at B23 of the Diamond Light Source. NMR data was obtained at the Henry Wellcome NMR centre at the University of Birmingham.

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Copyright Statement
Copyright information regarding this work can be found at the following address: http://creativecommons.org/licenses/by/4.0





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