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The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.

Authors :
Masson JY
Davies AA
Hajibagheri N
Van Dyck E
Benson FE
Stasiak AZ
Stasiak A
West SC
Source :
The EMBO journal [EMBO J] 1999 Nov 15; Vol. 18 (22), pp. 6552-60.
Publication Year :
1999

Abstract

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.

Details

Language :
English
ISSN :
0261-4189
Volume :
18
Issue :
22
Database :
MEDLINE
Journal :
The EMBO journal
Publication Type :
Academic Journal
Accession number :
10562567
Full Text :
https://doi.org/10.1093/emboj/18.22.6552