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

Jae Sung Woo; Jae Hong Lim; Ho Chul Shin; Min Kang Suh; Bonsu Ku; Kwang Hoon Lee; Keehyoung Joo; Howard Robinson; Jooyoung Lee; Sam Yong Park; Nam Chul Ha; Byung Ha Oh

doi:10.1016/j.cell.2008.10.050

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

Jae Sung Woo, Jae Hong Lim, Ho Chul Shin, Min Kang Suh, Bonsu Ku, Kwang Hoon Lee, Keehyoung Joo, Howard Robinson, Jooyoung Lee, Sam Yong Park, Nam Chul Ha, Byung Ha Oh

Research output: Contribution to journal › Article › peer-review

123 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	85-96
Number of pages	12
Journal	Cell
Volume	136
Issue number	1
DOIs	https://doi.org/10.1016/j.cell.2008.10.050
Publication status	Published - 2009 Jan 9
Externally published	Yes

Bibliographical note

Funding Information:
This study was supported by Creative Research Initiatives (Center for Biomolecular Interaction) of MOST/KOSEF and partly by Core Research Program of POSTECH. J.-H.L., M.-K.S., H.-C.S., B.K. and K.-H.L. were supported by the Brain Korea 21 Project. This study made use of the beamline 4A at the Pohang Accelerator Laboratory in Korea, the beamline BL-5A at Photon Factory in Japan and the Brookhaven National Laboratory/Biology beamline X29 at the National Synchrotron Light Source in USA. The BNL Biology/PX Mail-in program is supported by the NIH institute, National Center for Research Resources.

Keywords

CELLBIO
PROTEINS

ASJC Scopus subject areas

General Biochemistry,Genetics and Molecular Biology

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10.1016/j.cell.2008.10.050

Cite this

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title = "Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions",

abstract = "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.",

keywords = "CELLBIO, PROTEINS",

author = "Woo, {Jae Sung} and Lim, {Jae Hong} and Shin, {Ho Chul} and Suh, {Min Kang} and Bonsu Ku and Lee, {Kwang Hoon} and Keehyoung Joo and Howard Robinson and Jooyoung Lee and Park, {Sam Yong} and Ha, {Nam Chul} and Oh, {Byung Ha}",

note = "Funding Information: This study was supported by Creative Research Initiatives (Center for Biomolecular Interaction) of MOST/KOSEF and partly by Core Research Program of POSTECH. J.-H.L., M.-K.S., H.-C.S., B.K. and K.-H.L. were supported by the Brain Korea 21 Project. This study made use of the beamline 4A at the Pohang Accelerator Laboratory in Korea, the beamline BL-5A at Photon Factory in Japan and the Brookhaven National Laboratory/Biology beamline X29 at the National Synchrotron Light Source in USA. The BNL Biology/PX Mail-in program is supported by the NIH institute, National Center for Research Resources. ",

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AU - Woo, Jae Sung

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AU - Shin, Ho Chul

AU - Suh, Min Kang

AU - Ku, Bonsu

AU - Lee, Kwang Hoon

AU - Joo, Keehyoung

AU - Robinson, Howard

AU - Lee, Jooyoung

AU - Park, Sam Yong

AU - Ha, Nam Chul

AU - Oh, Byung Ha

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PY - 2009/1/9

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N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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