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Title: The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.
Authors: Fisher, GL
Pastrana, CL
Higman, VA
Koh, A
Taylor, JA
Butterer, A
Craggs, T
Sobott, F
Murray, H
Crump, MP
Moreno-Herrero, F
Dillingham, MS
First Published: 15-Dec-2017
Publisher: eLife Sciences Publications
Citation: Elife, 2017;6:e28086
Abstract: The ParB protein forms DNA bridging interactions around parS to condense DNA and earmark the bacterial chromosome for segregation. The molecular mechanism underlying the formation of these ParB networks is unclear. We show here that while the central DNA binding domain is essential for anchoring at parS, 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-GFP 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 in Bacillus subtilis.
DOI Link: 10.7554/eLife.28086
eISSN: 2050-084X
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2017. This is an open-access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Molecular and Cell Biology

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