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Asymmetric MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin

Katarzyna Zawadzka, Pawel Zawadzki, Rachel Baker, Karthik V. Rajasekar, David J. Sherratt, View ORCID ProfileLidia K. Arciszewska
doi: https://doi.org/10.1101/180729
Katarzyna Zawadzka
1present address: Department of Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznan, Poland
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Pawel Zawadzki
2present address: Division of Molecular Biophysics, Adam Mickiewicz University Umultowska 85, 61-614 Poznan, Poland
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Rachel Baker
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Karthik V. Rajasekar
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David J. Sherratt
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Lidia K. Arciszewska
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  • ORCID record for Lidia K. Arciszewska
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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, forming an asymmetric tripartite complex, as in other SMC complexes. Since MukF dimerization is preserved during this interaction, MukF directs the formation of dimer of dimers MukBEF complexes, observed previously in vivo. The MukF N- and C-terminal domains stimulate ATPase independently and additively, consistent with them each targeting only one of the two MukB ATPase active sites in the asymmetric complex. We demonstrate that MukF interaction with the MukB neck turns over during cycles of ATP binding and hydrolysis in vivo and that impairment of this interaction leads to MukBEF release from chromosomes.

Footnotes

  • ↵* communicating authors: david.sherratt{at}bioch.ox.ac.uk; lidia.arciszewska{at}bioch.ox.ac.uk

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted August 25, 2017.
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Asymmetric MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
Katarzyna Zawadzka, Pawel Zawadzki, Rachel Baker, Karthik V. Rajasekar, David J. Sherratt, Lidia K. Arciszewska
bioRxiv 180729; doi: https://doi.org/10.1101/180729
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Asymmetric MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
Katarzyna Zawadzka, Pawel Zawadzki, Rachel Baker, Karthik V. Rajasekar, David J. Sherratt, Lidia K. Arciszewska
bioRxiv 180729; doi: https://doi.org/10.1101/180729

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