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...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
eLife Sciences Publications
2018
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| _version_ | 1826288973405749248 |
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| author | Zawadzka, K Zawadzki, P Baker, R Rajasekar, K Wagner, F Sherratt, D Arciszewska, L |
| author_facet | Zawadzka, K Zawadzki, P Baker, R Rajasekar, K Wagner, F Sherratt, D Arciszewska, L |
| author_sort | Zawadzka, K |
| collection | OXFORD |
| 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. |
| first_indexed | 2024-03-07T02:21:49Z |
| format | Journal article |
| id | oxford-uuid:a431826b-2d26-4396-a3f6-58400c57875b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:21:49Z |
| publishDate | 2018 |
| publisher | eLife Sciences Publications |
| record_format | dspace |
| spelling | oxford-uuid:a431826b-2d26-4396-a3f6-58400c57875b2022-03-27T02:32:07ZMukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisinJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a431826b-2d26-4396-a3f6-58400c57875bEnglishSymplectic Elements at OxfordeLife Sciences Publications2018Zawadzka, KZawadzki, PBaker, RRajasekar, KWagner, FSherratt, DArciszewska, LThe 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. |
| spellingShingle | Zawadzka, K Zawadzki, P Baker, R Rajasekar, K Wagner, F Sherratt, D Arciszewska, L 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 |
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