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

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 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 com...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

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Publisher copy:
10.7554/eLife.31522

Authors


Zawadzka, K More by this author
Zawadzki, P More by this author
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
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ORCID:
0000-0002-8146-6560
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
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Funding agency for:
Sherratt, DJ
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Funding agency for:
Sherratt, DJ
Publisher:
eLife Sciences Publications Publisher's website
Journal:
eLife Journal website
Volume:
7
Pages:
Article: e31522
Publication date:
2018-01-11
Acceptance date:
2018-01-10
DOI:
ISSN:
2050-084X
Pubs id:
pubs:819987
URN:
uri:a431826b-2d26-4396-a3f6-58400c57875b
UUID:
uuid:a431826b-2d26-4396-a3f6-58400c57875b
Local pid:
pubs:819987

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