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The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.
- 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.
- Subjects :
- Adenosine Triphosphatases isolation & purification
Cloning, Molecular
DNA Nucleotidyltransferases isolation & purification
DNA, Single-Stranded biosynthesis
DNA, Single-Stranded chemistry
DNA, Viral biosynthesis
DNA, Viral chemistry
DNA-Binding Proteins isolation & purification
Escherichia coli genetics
Gene Library
Humans
Male
Meiosis
Microscopy, Electron
Nucleic Acid Heteroduplexes biosynthesis
Nucleic Acid Heteroduplexes chemistry
Organ Specificity
Rad51 Recombinase
Rec A Recombinases metabolism
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Recombinant Proteins ultrastructure
Recombinases
Recombination, Genetic
Testis enzymology
Adenosine Triphosphatases metabolism
Adenosine Triphosphatases ultrastructure
Cell Cycle Proteins
DNA Nucleotidyltransferases metabolism
DNA Nucleotidyltransferases ultrastructure
DNA-Binding Proteins chemistry
DNA-Binding Proteins metabolism
DNA-Binding Proteins ultrastructure
Integrases
Subjects
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