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

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 dimer...

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Autores principales: Zawadzka, Katarzyna, Zawadzki, Pawel, Baker, Rachel, Rajasekar, Karthik V, Wagner, Florence, Sherratt, David J, Arciszewska, Lidia K
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5812716/
https://www.ncbi.nlm.nih.gov/pubmed/29323635
http://dx.doi.org/10.7554/eLife.31522
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author Zawadzka, Katarzyna
Zawadzki, Pawel
Baker, Rachel
Rajasekar, Karthik V
Wagner, Florence
Sherratt, David J
Arciszewska, Lidia K
author_facet Zawadzka, Katarzyna
Zawadzki, Pawel
Baker, Rachel
Rajasekar, Karthik V
Wagner, Florence
Sherratt, David J
Arciszewska, Lidia K
author_sort Zawadzka, Katarzyna
collection PubMed
description 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 dimerisation 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 dimerisation 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.
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spelling pubmed-58127162018-02-16 MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin Zawadzka, Katarzyna Zawadzki, Pawel Baker, Rachel Rajasekar, Karthik V Wagner, Florence Sherratt, David J Arciszewska, Lidia K eLife Genes and Chromosomes 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 dimerisation 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 dimerisation 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. eLife Sciences Publications, Ltd 2018-01-11 /pmc/articles/PMC5812716/ /pubmed/29323635 http://dx.doi.org/10.7554/eLife.31522 Text en © 2018, Zawadzka et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Genes and Chromosomes
Zawadzka, Katarzyna
Zawadzki, Pawel
Baker, Rachel
Rajasekar, Karthik V
Wagner, Florence
Sherratt, David J
Arciszewska, Lidia K
MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
title MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
title_full MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
title_fullStr MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
title_full_unstemmed MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
title_short MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
title_sort mukb atpases are regulated independently by the n- and c-terminal domains of mukf kleisin
topic Genes and Chromosomes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5812716/
https://www.ncbi.nlm.nih.gov/pubmed/29323635
http://dx.doi.org/10.7554/eLife.31522
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