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

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...

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Autores principales: Hyde, Eva I., Callow, Philip, Rajasekar, Karthik V., Timmins, Peter, Patel, Trushar R., Siligardi, Giuliano, Hussain, Rohanah, White, Scott A., Thomas, Christopher M., Scott, David J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577506/
https://www.ncbi.nlm.nih.gov/pubmed/28760886
http://dx.doi.org/10.1042/BCJ20170281
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author Hyde, Eva I.
Callow, Philip
Rajasekar, Karthik V.
Timmins, Peter
Patel, Trushar R.
Siligardi, Giuliano
Hussain, Rohanah
White, Scott A.
Thomas, Christopher M.
Scott, David J.
author_facet Hyde, Eva I.
Callow, Philip
Rajasekar, Karthik V.
Timmins, Peter
Patel, Trushar R.
Siligardi, Giuliano
Hussain, Rohanah
White, Scott A.
Thomas, Christopher M.
Scott, David J.
author_sort Hyde, Eva I.
collection PubMed
description 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.
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spelling pubmed-55775062017-09-01 Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA Hyde, Eva I. Callow, Philip Rajasekar, Karthik V. Timmins, Peter Patel, Trushar R. Siligardi, Giuliano Hussain, Rohanah White, Scott A. Thomas, Christopher M. Scott, David J. Biochem J Research Articles 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. Portland Press Ltd. 2017-09-15 2017-08-31 /pmc/articles/PMC5577506/ /pubmed/28760886 http://dx.doi.org/10.1042/BCJ20170281 Text en © 2017 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Articles
Hyde, Eva I.
Callow, Philip
Rajasekar, Karthik V.
Timmins, Peter
Patel, Trushar R.
Siligardi, Giuliano
Hussain, Rohanah
White, Scott A.
Thomas, Christopher M.
Scott, David J.
Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
title Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
title_full Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
title_fullStr Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
title_full_unstemmed Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
title_short Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA
title_sort intrinsic disorder in the partitioning protein korb persists after co-operative complex formation with operator dna and kora
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577506/
https://www.ncbi.nlm.nih.gov/pubmed/28760886
http://dx.doi.org/10.1042/BCJ20170281
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