Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions

Condensins are key mediators of chromosome condensation across organisms. Like other condensins, the bacterial MukBEF condensin complex consists of an SMC family protein dimer containing two ATPase head domains, MukB, and two interacting subunits, MukE and MukF. We report complete structural views o...

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Bibliographic Details
Published in:Cell 2009-01, Vol.136 (1), p.85-96
Main Authors: Woo, Jae-Sung, Lim, Jae-Hong, Shin, Ho-Chul, Suh, Min-Kang, Ku, Bonsu, Lee, Kwang-Hoon, Joo, Keehyoung, Robinson, Howard, Lee, Jooyoung, Park, Sam-Yong, Ha, Nam-Chul, Oh, Byung-Ha
Format: Article
Language:English
Subjects:
59
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate
Bacteria
Bacteria - chemistry
Bacteria - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Binding Sites
CELLBIO
DNA - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Models, Molecular
Multiprotein Complexes - chemistry
Multiprotein Complexes - metabolism
Protein Structure, Tertiary
PROTEINS
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Summary:Condensins are key mediators of chromosome condensation across organisms. Like other condensins, the bacterial MukBEF condensin complex consists of an SMC family protein dimer containing two ATPase head domains, MukB, and two interacting subunits, MukE and MukF. We report complete structural views of the intersubunit interactions of this condensin along with ensuing studies that reveal a role for the ATPase activity of MukB. MukE and MukF together form an elongated dimeric frame, and MukF's C-terminal winged-helix domains (C-WHDs) bind MukB heads to constitute closed ring-like structures. Surprisingly, one of the two bound C-WHDs is forced to detach upon ATP-mediated engagement of MukB heads. This detachment reaction depends on the linker segment preceding the C-WHD, and mutations on the linker restrict cell growth. Thus ATP-dependent transient disruption of the MukB-MukF interaction, which creates openings in condensin ring structures, is likely to be a critical feature of the functional mechanism of condensins.
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2008.10.050