Identification and purification of two distinct complexes containing the five RAD51 paralogs.

Détails

ID Serval
serval:BIB_12EC1D985834
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Identification and purification of two distinct complexes containing the five RAD51 paralogs.
Périodique
Genes and Development
Auteur⸱e⸱s
Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R., McIlwraith M.J., Benson F.E., West S.C.
ISSN
0890-9369 (Print)
ISSN-L
0890-9369
Statut éditorial
Publié
Date de publication
12/2001
Volume
15
Numéro
24
Pages
3296-3307
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Cells defective in any of the RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, and XRCC3) are sensitive to DNA cross-linking agents and to ionizing radiation. Because the paralogs are required for the assembly of DNA damage-induced RAD51 foci, and mutant cell lines are defective in homologous recombination and show genomic instability, their defect is thought to be caused by an inability to promote efficient recombinational repair. Here, we show that the five paralogs exist in two distinct complexes in human cells: one contains RAD51B, RAD51C, RAD51D, and XRCC2 (defined as BCDX2), whereas the other consists of RAD51C with XRCC3. Both protein complexes have been purified to homogeneity and their biochemical properties investigated. BCDX2 binds single-stranded DNA and single-stranded gaps in duplex DNA, in accord with the proposal that the paralogs play an early (pre-RAD51) role in recombinational repair. Moreover, BCDX2 complex binds specifically to nicks in duplex DNA. We suggest that the extreme sensitivity of paralog-defective cell lines to cross-linking agents is owing to defects in the processing of incised cross links and the consequential failure to initiate recombinational repair at these sites.
Mots-clé
Adenosine Triphosphatases/metabolism, Baculoviridae/genetics, Chromatography, Gel, DNA Repair/genetics, DNA Repair/physiology, DNA, Single-Stranded/metabolism, DNA-Binding Proteins/isolation & purification, DNA-Binding Proteins/metabolism, Humans, Male, Microscopy, Electron, Precipitin Tests, Protein Binding, Protein Isoforms/isolation & purification, Protein Isoforms/metabolism, Rad51 Recombinase, Recombinant Proteins/metabolism, Recombination, Genetic, Testis/chemistry, Testis/cytology
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
20/08/2019 13:41
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