MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
- University of Oxford, United Kingdom
Abstract
The Escherichia coli SMC complex, MukBEF, acts in chromosome segregation. MukBEF shares the distinctive architecture of other SMC complexes, with one prominent difference; unlike other kleisins, MukF forms dimers through its N-terminal domain. We show that a 4-helix bundle adjacent to the MukF dimerization domain interacts functionally with the MukB coiled-coiled 'neck' adjacent to the ATPase head. We propose that this interaction leads to an asymmetric tripartite complex, as in other SMC complexes. Since MukF dimerization is preserved during this interaction, MukF directs the formation of dimer of dimer MukBEF complexes, observed previously in vivo. The MukF N- and C-terminal domains stimulate MukB ATPase independently and additively. We demonstrate that impairment of the MukF interaction with MukB in vivo leads to ATP hydrolysis-dependent release of MukBEF complexes from chromosomes.
Article and author information
Author details
Karthik V Rajasekar
Lidia K Arciszewska
Funding
Wellcome (Senior Investigator Award)
- David J Sherratt
Leverhulme Trust (RP2013-K-017)
- David J Sherratt
National Science Centre, Poland (2015/19/P/NZ1/03859)
- Pawel Zawadzki
Foundation for Polish Science (First TEAM/2016-1/9)
- Pawel Zawadzki
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2018, Zawadzka et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
eLife 7:e31522.
https://doi.org/10.7554/eLife.31522
