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Eukaryotic Rad50 functions as a rod-shaped dimer

  • 저널명Nat Struct Mol Biol (2017) Mar;24(3):248-257
    • 담당교수Yunje Cho
    • 조회975
    • 작성자최고관리자
    • 2017-09-28



    The Rad50 hook interface is crucial for assembly and various functions of the Mre11 complex. Previous analyses suggested that
    Rad50 molecules interact within (intracomplex) or between (intercomplex) dimeric complexes. In this study, we determined the
    structure of the human Rad50 hook and coiled-coil domains. The data suggest that the predominant structure is the intracomplex,
    in which the two parallel coiled coils proximal to the hook form a rod shape, and that a novel interface within the coiled-coil
    domains of Rad50 stabilizes the interaction of Rad50 protomers in the dimeric assembly. In yeast, removal of the coiled-coil
    interface compromised Tel1 activation without affecting DNA repair, while simultaneous disruption of that interface and the
    hook phenocopied a null mutation. The results demonstrate that the hook and coiled-coil interfaces coordinately promote
    intracomplex assembly and define the intracomplex as the functional form of the Mre11 complex.