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

Détails

ID Serval
serval:BIB_84CEE07392BB
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.
Périodique
Embo Journal
Auteur(s)
Masson J.Y., Davies A.A., Hajibagheri N., Van Dyck E., Benson F.E., Stasiak A.Z., Stasiak A., West S.C.
ISSN
0261-4189 (Print)
ISSN-L
0261-4189
Statut éditorial
Publié
Date de publication
1999
Volume
18
Numéro
22
Pages
6552-6560
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
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.
Mots-clé
Adenosine Triphosphatases/isolation & purification, Adenosine Triphosphatases/metabolism, Cell Cycle Proteins, Cloning, Molecular, DNA Nucleotidyltransferases/isolation & purification, DNA Nucleotidyltransferases/metabolism, DNA, Single-Stranded/biosynthesis, DNA, Single-Stranded/chemistry, DNA, Viral/biosynthesis, DNA, Viral/chemistry, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/isolation & purification, Escherichia coli/genetics, Gene Library, Humans, Integrases, 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, Recombinases, Recombination, Genetic, Testis/enzymology
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
08/05/2019 21:21
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