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The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.pdf (5.93 MB)

The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.

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posted on 2019-06-18, 15:11 authored by GL Fisher, CL Pastrana, VA Higman, A Koh, JA Taylor, A Butterer, T Craggs, F Sobott, H Murray, MP Crump, F Moreno-Herrero, MS Dillingham
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.

Funding

GLMF was supported by the Biotechnology and Biological Sciences Research Council (1363883). MSD, JAT, VAH and TDC were supported by the Wellcome Trust (100401 and 077368). FMH acknowledges support from the European Research Council (681299) and from MINECO (FIS2014-58328-P). HM was supported by The Royal Society.

History

Citation

Elife, 2017;6:e28086

Author affiliation

/Organisation/COLLEGE OF LIFE SCIENCES/Biological Sciences/Molecular & Cell Biology

Version

  • VoR (Version of Record)

Published in

Elife

Publisher

eLife Sciences Publications

eissn

2050-084X

Acceptance date

2017-12-02

Copyright date

2017

Available date

2019-06-18

Publisher version

https://elifesciences.org/articles/28086

Language

en

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