Order and disorder in the domain organization of the plasmid partition protein KorB

Karthik Rajasekar, Sidra Tul Muntaha, Jeremy R.H. Tame, Sireesha Kommareddy, Gordon Morris, Christopher W. Wharton, Christopher M. Thomas, Scott A. White, Eva I. Hyde, David J. Scott

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)15440-15449
Number of pages10
JournalJournal of Biological Chemistry
Issue number20
Publication statusPublished - 14 May 2010
Externally publishedYes


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