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. 2007 Apr 10;5(5):e105. doi: 10.1371/journal.pbio.0050105

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This is an open-access article distributed under the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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All DMC1 protein in this figure is human, and A272P refers to the human protein containing the DMC1^Mei11 amino acid alteration.

(A) Coomassie blue–stained gel showing the bacterially produced and purified wt and mutant proteins.

(B) Both wt and mutant show preferential binding to ssDNA. Shown is a gel shift assay in which the indicated amounts of wt or mutant protein (A272P) was incubated with a mixture of single-stranded and double-stranded 100-mer oligonucleotides.

(C) The extent of DNA binding for the single-stranded 100-mer. This is a graph of the raw data in (B).

(D) The mutant protein is deficient in D-loop formation. The D-loop assay was carried out as described in the absence or presence of cofactor HOP2-MND1 complex.