Fisher, G.L.M., Pastrana, C.L., Higman, V.A. et al. (9 more authors) (2017) The C-terminal domain Of ParB Is critical for dynamic DNA binding and bridging interactions which condense the bacterial centromere. eLife, 6. e28086.
Abstract
The ParB protein forms DNA bridging interactions around parS to form networks which condense DNA and earmark the bacterial chromosome for segregation. The mechanism underlying the formation of ParB nucleoprotein complexes is unclear. We show here that the central DNA binding domain is essential for anchoring at parS, and that this interaction is not required for DNA condensation. Structural analysis of the C-terminal domain reveals a dimer with a lysine-rich surface that binds DNA non-specifically and is essential for DNA condensation in vitro. Mutation of either the dimerisation or the DNA binding interface eliminates ParB foci formation in vivo. Moreover, the free C-terminal domain can rapidly decondense ParB networks independently of its ability to bind DNA. Our work reveals a dual role for the C-terminal domain of ParB as both a DNA binding and bridging interface, and highlights the dynamic nature of ParB networks.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Editors: |
|
Copyright, Publisher and Additional Information: | © Copyright Fisher et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. |
Dates: |
|
Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 22 Dec 2017 11:53 |
Last Modified: | 06 Nov 2018 13:56 |
Published Version: | https://doi.org/10.7554/eLife.28086 |
Status: | Published |
Publisher: | eLife Sciences Publications Ltd |
Refereed: | Yes |
Identification Number: | 10.7554/eLife.28086 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:125118 |