Activation of human meiosis-specific recombinase Dmc1 by Ca2+.

Details

Serval ID
serval:BIB_E59B2CB2B388
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Activation of human meiosis-specific recombinase Dmc1 by Ca2+.
Journal
Journal of Biological Chemistry
Author(s)
Bugreev D.V., Golub E.I., Stasiak A.Z., Stasiak A., Mazin A.V.
ISSN
0021-9258[print], 0021-9258[linking]
Publication state
Published
Issued date
2005
Peer-reviewed
Oui
Volume
280
Number
29
Pages
26886-26895
Language
english
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Abstract
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.
Keywords
Adenosine Triphosphatases/metabolism, Adenosine Triphosphate, Binding Sites, Calcium/metabolism, Calcium/pharmacology, Cell Cycle Proteins/metabolism, Crossing Over, Genetic, DNA, Single-Stranded, DNA-Binding Proteins/metabolism, Enzyme Activation, Humans, Magnesium/pharmacology, Meiosis, Protein Conformation/drug effects, Rad51 Recombinase, Recombinases, Recombination, Genetic
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 10:35
Last modification date
20/08/2019 16:08
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