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Activation of human meiosis-specific recombinase Dmc1 by Ca2
Journal article   Open access   Peer reviewed

Activation of human meiosis-specific recombinase Dmc1 by Ca2

Dmitry V Bugreev, Efim I Golub, Alicja Z Stasiak, Andrzej Stasiak and Alexander V Mazin
The Journal of biological chemistry, v 280(29), pp 26886-26895
22 Jul 2005
DOI: https://doi.org/10.1074/jbc.M502248200
PMID: 15917244
Featured in Collection :   UN Sustainable Development Goals @ Drexel
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https://doi.org/10.1074/jbc.M502248200View
Published, Version of Record (VoR) Open

Abstract

Calcium - pharmacology Crossing Over, Genetic Rad51 Recombinase Calcium - metabolism Humans Protein Conformation - drug effects Recombinases Cell Cycle Proteins - metabolism Adenosine Triphosphatases - metabolism Meiosis Adenosine Triphosphate Magnesium - pharmacology DNA-Binding Proteins - metabolism Recombination, Genetic DNA, Single-Stranded Enzyme Activation Binding Sites
Rad51 and its meiotic homolog Dmc1 are key proteins of homologous recombination in eukaryotes. These proteins form nucleoprotein complexes on single-stranded DNA that promote a search for homology and that perform DNA strand exchange, the two essential steps of genetic recombination. Previously, we demonstrated that Ca2+ greatly stimulates the DNA strand exchange activity of human (h) Rad51 protein (Bugreev, D. V., and Mazin, A. V. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 9988-9993). Here, we show that the DNA strand exchange activity of hDmc1 protein is also stimulated by Ca2+. However, the mechanism of stimulation of hDmc1 protein appears to be different from that of hRad51 protein. In the case of hRad51 protein, Ca2+ acts primarily by inhibiting its ATPase activity, thereby preventing self-conversion into an inactive ADP-bound complex. In contrast, we demonstrate that hDmc1 protein does not self-convert into a stable ADP-bound complex. The results indicate that activation of hDmc1 is mediated through conformational changes induced by free Ca2+ ion binding to a protein site that is distinct from the Mg2+.ATP-binding center. These conformational changes are manifested by formation of more stable filamentous hDmc1.single-stranded DNA complexes. Our results demonstrate a universal role of Ca2+ in stimulation of mammalian DNA strand exchange proteins and reveal diversity in the mechanisms of this stimulation.

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Web of Science research areas
Biochemistry & Molecular Biology
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