Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB

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Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB. / Rajasekar, Karthik; Muntaha, Sidra-Tul; Tame, JRH; Kommareddy, Sireesha; Morris, G; Wharton, Christopher; Thomas, Christopher; White, Scott; Hyde, Eva; Scott, DJ.

In: Journal of Biological Chemistry, Vol. 285, No. 20, 01.05.2010, p. 15440-15449.

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Rajasekar, Karthik ; Muntaha, Sidra-Tul ; Tame, JRH ; Kommareddy, Sireesha ; Morris, G ; Wharton, Christopher ; Thomas, Christopher ; White, Scott ; Hyde, Eva ; Scott, DJ. / Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB. In: Journal of Biological Chemistry. 2010 ; Vol. 285, No. 20. pp. 15440-15449.

Bibtex

@article{8ca8162d28c74513a9d8e54277373770,
title = "Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB",
abstract = "The plasmid partition protein KorB has a dual role: it is essential for the correct segregation of the low copy number broad host range RK2 plasmid while also being an important regulator of transcription. KorB belongs to the ParB family of proteins, and partitioning in RK2 has been studied as a simplified model of bacterial chromosome segregation. Structural information on full-length ParB proteins is limited, mainly due to the inability to grow crystals suitable for diffraction studies. We show, using CD and NMR, that KorB has regions of significant intrinsic disorder and hence it adopts a multiplicity of conformations in solution. The biophysical data are consistent with bioinformatic predictions based on the amino acid sequence that the N-terminal region and also the region between the central DNA-binding domain and the C-terminal dimerization domain are intrinsically disordered. We have used small angle x-ray scattering data to determine the ensemble of solution conformations for KorB and selected deletion mutants, based on models of the known domain structures. This conformational range of KorB is likely to be biologically required for DNA partitioning and for binding to a diverse set of partner proteins.",
author = "Karthik Rajasekar and Sidra-Tul Muntaha and JRH Tame and Sireesha Kommareddy and G Morris and Christopher Wharton and Christopher Thomas and Scott White and Eva Hyde and DJ Scott",
year = "2010",
month = may,
day = "1",
doi = "10.1074/jbc.M109.096099",
language = "English",
volume = "285",
pages = "15440--15449",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "20",

}

RIS

TY - JOUR

T1 - Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB

AU - Rajasekar, Karthik

AU - Muntaha, Sidra-Tul

AU - Tame, JRH

AU - Kommareddy, Sireesha

AU - Morris, G

AU - Wharton, Christopher

AU - Thomas, Christopher

AU - White, Scott

AU - Hyde, Eva

AU - Scott, DJ

PY - 2010/5/1

Y1 - 2010/5/1

N2 - The plasmid partition protein KorB has a dual role: it is essential for the correct segregation of the low copy number broad host range RK2 plasmid while also being an important regulator of transcription. KorB belongs to the ParB family of proteins, and partitioning in RK2 has been studied as a simplified model of bacterial chromosome segregation. Structural information on full-length ParB proteins is limited, mainly due to the inability to grow crystals suitable for diffraction studies. We show, using CD and NMR, that KorB has regions of significant intrinsic disorder and hence it adopts a multiplicity of conformations in solution. The biophysical data are consistent with bioinformatic predictions based on the amino acid sequence that the N-terminal region and also the region between the central DNA-binding domain and the C-terminal dimerization domain are intrinsically disordered. We have used small angle x-ray scattering data to determine the ensemble of solution conformations for KorB and selected deletion mutants, based on models of the known domain structures. This conformational range of KorB is likely to be biologically required for DNA partitioning and for binding to a diverse set of partner proteins.

AB - The plasmid partition protein KorB has a dual role: it is essential for the correct segregation of the low copy number broad host range RK2 plasmid while also being an important regulator of transcription. KorB belongs to the ParB family of proteins, and partitioning in RK2 has been studied as a simplified model of bacterial chromosome segregation. Structural information on full-length ParB proteins is limited, mainly due to the inability to grow crystals suitable for diffraction studies. We show, using CD and NMR, that KorB has regions of significant intrinsic disorder and hence it adopts a multiplicity of conformations in solution. The biophysical data are consistent with bioinformatic predictions based on the amino acid sequence that the N-terminal region and also the region between the central DNA-binding domain and the C-terminal dimerization domain are intrinsically disordered. We have used small angle x-ray scattering data to determine the ensemble of solution conformations for KorB and selected deletion mutants, based on models of the known domain structures. This conformational range of KorB is likely to be biologically required for DNA partitioning and for binding to a diverse set of partner proteins.

U2 - 10.1074/jbc.M109.096099

DO - 10.1074/jbc.M109.096099

M3 - Article

C2 - 20200158

VL - 285

SP - 15440

EP - 15449

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 20

ER -