TAILIEUCHUNG - Báo cáo khoa học: Focal localization of MukBEF condensin on the chromosome requires the flexible linker region of MukF

Condensin complexes are the key mediators of chromosome condensation. The MukB–MukE–MukF complex is a bacterial condensin, in which the MukB subunit forms a V-shaped dimeric structure with two ATPase head domains. MukE and MukF together form a tight complex, which binds to the MukB head via the C-terminal winged-helix domain (C-WHD) of MukF. | ỊFEBS Journal Focal localization of MukBEF condensin on the chromosome requires the flexible linker region of MukF Ho-Chul Shin1 Jae-Hong Lim2 Jae-Sung Woo1 and Byung-Ha Oh1 1 Center for Biomolecular Recognition and Division of Molecular and Life Science Pohang University of Science and Technology Korea 2 Beanline Division Pohang Accelerator Laboratory Korea Keywords chromosome condensation condensing kleisin complex MukBEF complex SMC protein Correspondence . Oh Department of Life Sciences Center for Biomolecular Recognition and Division of Molecular and Life Science Pohang University of Science and Technology Pohang Kyungbuk 790-784 Korea Fax 82 54 279 2199 Tel 82 54 279 2289 E-mail bhoh@ Received 13 April2009 revised 5 July 2009 accepted 8 July 2009 doi Condensin complexes are the key mediators of chromosome condensation. The MukB-MukE-MukF complex is a bacterial condensin in which the MukB subunit forms a V-shaped dimeric structure with two ATPase head domains. MukE and MukF together form a tight complex which binds to the MukB head via the C-terminal winged-helix domain C-WHD of MukF. One of the two bound C-WHDs of MukF is forced to detach from two ATP-bound engaged MukB heads and this detachment reaction depends on the MukF flexible linker preceding the C-WHD. Whereas MukB is known to focally localize at particular positions in cells by an unknown mechanism mukE- or mukF-null mutation causes MukB to become dispersed in cells. Here we report that mutations in MukF causing a defect in the detachment reaction interfere with the focal localization of MukB and that the dispersed distribution of MukB in cells correlates directly with defects in cell growth and division. The data strongly suggest that the MukB-MukE-MukF condensin forms huge clusters through the ATP-dependent detachment reaction and this cluster formation is critical for chromosome condensation by this machinery. We also show that the MukF flexible .

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