Masson, J. Y. and Davies, A. A. and Hajibagheri, N. and Van Dyck, E. and Benson, Fiona E. and Stasiak, A. Z. and Stasiak, A. and West, S. C. (1999) The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51. EMBO Journal, 18 (22). pp. 6552-6560. ISSN 0261-4189Full text not available from this repository.
Eukaryotic cells encode two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, which are required for meiotic recombination. Rad51, like E.coli RecA, forms helical nucleoprotein filaments that promote joint molecule and heteroduplex DNA formation. Electron microscopy reveals that the human meiosis-specific recombinase Dmc1 forms ring structures that bind single-stranded (ss) and double-stranded (ds) DNA. The protein binds preferentially to ssDNA tails and gaps in duplex DNA. hDmc1–ssDNA complexes exhibit an irregular, often compacted structure, and promote strand-transfer reactions with homologous duplex DNA. hDmc1 binds duplex DNA with reduced affinity to form nucleoprotein complexes. In contrast to helical RecA/Rad51 filaments, however, Dmc1 filaments are composed of a linear array of stacked protein rings. Consistent with the requirement for two recombinases in meiotic recombination, hDmc1 interacts directly with hRad51.
|Journal or Publication Title:||EMBO Journal|
|Uncontrolled Keywords:||hDmc1 ; hRad51 ; meiotic recombination ; recombinases ; ring structures|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited By:||Dr Fiona E Benson|
|Deposited On:||21 May 2008 16:22|
|Last Modified:||24 Feb 2017 00:39|
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