Structural Basis for Octameric Ring Formation and DNA Interaction of the Human Homologous-Pairing Protein Dmc1

• Published in: Molecular cell Vol. 14; no. 3; pp. 363 - 374
• Main Authors: Kinebuchi, Takashi, Kagawa, Wataru, Enomoto, Rima, Tanaka, Kozo, Miyagawa, Kiyoshi, Shibata, Takehiko, Kurumizaka, Hitoshi, Yokoyama, Shigeyuki
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07.05.2004
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Animals; Binding Sites - genetics; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - genetics; Chromosome Segregation - genetics; Crystallography, X-Ray; DNA - chemistry; DNA - genetics; DNA, Single-Stranded - chemistry; DNA, Single-Stranded - genetics; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; Humans; Macromolecular Substances; Meiosis - genetics; Models, Molecular; Molecular Weight; Protein Conformation; Protein Structure, Tertiary - genetics; Recombination, Genetic - genetics; Sequence Homology

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 D...