Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1

Takashi Kinebuchi, Wataru Kagawa, Rima Enomoto, Kozo Tanaka, Kiyoshi Miyagawa, Takehiko Shibata, Hitoshi Kurumizaka, Shigeyuki Yokoyama

    Research output: Contribution to journalArticle

    89 Citations (Scopus)

    Abstract

    The human Dmc1 protein, a RecA/Rad51 homolog, is a meiosis-specific DNA recombinase that catalyzes homologous pairing. RecA and Rad51 form helical filaments, while Dmc1 forms an octameric ring. In the present study, we crystallized the full-length human Dmc1 protein and solved the structure of the Dmc1 octameric ring. The monomeric structure of the Dmc1 protein closely resembled those of the human and archaeal Rad51 proteins. In addition to the polymerization motif that was previously identified in the Rad51 proteins, we found another hydrogen bonding interaction at the polymer interface, which could explain why Dmc1 forms stable octameric rings instead of helical filaments. Mutagenesis studies identified the inner and outer basic patches that are important for homologous pairing. The inner patch binds both single-stranded and double-stranded DNAs, while the outer one binds single-stranded DNA. Based on these results, we propose a model for the interaction of the Dmc1 rings with DNA.

    Original languageEnglish
    Pages (from-to)363-374
    Number of pages12
    JournalMolecular Cell
    Volume14
    Issue number3
    DOIs
    Publication statusPublished - 2004 May 7

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    DNA
    Archaeal Proteins
    Rec A Recombinases
    Recombinases
    Proteins
    Single-Stranded DNA
    Meiosis
    Hydrogen Bonding
    Mutagenesis
    Polymerization
    Polymers

    ASJC Scopus subject areas

    • Molecular Biology

    Cite this

    Kinebuchi, T., Kagawa, W., Enomoto, R., Tanaka, K., Miyagawa, K., Shibata, T., ... Yokoyama, S. (2004). Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. Molecular Cell, 14(3), 363-374. https://doi.org/10.1016/S1097-2765(04)00218-7

    Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. / Kinebuchi, Takashi; Kagawa, Wataru; Enomoto, Rima; Tanaka, Kozo; Miyagawa, Kiyoshi; Shibata, Takehiko; Kurumizaka, Hitoshi; Yokoyama, Shigeyuki.

    In: Molecular Cell, Vol. 14, No. 3, 07.05.2004, p. 363-374.

    Research output: Contribution to journalArticle

    Kinebuchi, T, Kagawa, W, Enomoto, R, Tanaka, K, Miyagawa, K, Shibata, T, Kurumizaka, H & Yokoyama, S 2004, 'Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1', Molecular Cell, vol. 14, no. 3, pp. 363-374. https://doi.org/10.1016/S1097-2765(04)00218-7
    Kinebuchi, Takashi ; Kagawa, Wataru ; Enomoto, Rima ; Tanaka, Kozo ; Miyagawa, Kiyoshi ; Shibata, Takehiko ; Kurumizaka, Hitoshi ; Yokoyama, Shigeyuki. / Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. In: Molecular Cell. 2004 ; Vol. 14, No. 3. pp. 363-374.
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