Calcium ion promotes yeast Dmc1 activity via formation of long and fine helical filaments with single-stranded DNA

doi:10.1074/jbc.M505896200

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Papers In Press, published online ahead of print October 4, 2005
J. Biol. Chem, 10.1074/jbc.M505896200
Submitted on May 31, 2005
Revised on September 26, 2005
Accepted on October 3, 2005

Calcium ion promotes yeast Dmc1 activity via formation of long and fine helical filaments with single-stranded DNA

Ming-Hui Lee, Yuan-Chih Chang, Eurie L. Hong, Jennifer Grubb, Chia-Seng Chang, Douglas K. Bishop, and Ting-Fang Wang

Institute of Biological Chemistry, Academia Sinica, Taipei, Nankang 115

Corresponding Author: tfwang{at}gate.sinica.edu.tw

Dmc1 is specifically required for homologous recombination during meiosis. Here we report that Ca2+ promotes higher levels of Dmc1 strand assimilation activity than Mg2+. Relative to Mg2+, Ca2+ increases the affinity of Dmc1 for ATP and but reduces its DNA-dependent ATPase activity. These effects, together with previous studies of other RecA-like recombinases, support the view that ATP binding to Dmc1 protomers is required for functional filament structure. The helical pitch of ScDmc1-ssDNA helical filament was estimated to be 13.4 +/- 2.5 nm. Analysis of apparently “complete” Dmc1-ssDNA filaments indicated a stoichiometry of 24 +/- 2 nucleotides per turn of the Dmc1 helix. This finding suggests that the number or protomers per helical turn and/or the number of nucleotides bound per Dmc1 protomer differs from that reported previously for Rad51 and RecA filaments. Our data support the view that the active form of Dmc1 protein is a helical filament rather than a ring. We speculate that Ca2+ plays a significant role in regulating meiotic recombination.

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