Cargando…
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...
Autores principales: | , , , , , , |
---|---|
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 |
_version_ | 1783300074449666048 |
---|---|
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. |
format | Online Article Text |
id | pubmed-5812716 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT zawadzkakatarzyna mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin AT zawadzkipawel mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin AT bakerrachel mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin AT rajasekarkarthikv mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin AT wagnerflorence mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin AT sherrattdavidj mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin AT arciszewskalidiak mukbatpasesareregulatedindependentlybythenandcterminaldomainsofmukfkleisin |