Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex.
The Xrcc2 and Rad51D/Rad51L3 proteins, which belong to the Rad51 paralogs, are required for homologous recombinational repair (HRR) in vertebrates. The Xrcc2 and Rad51D/Rad51L3 genes, whose products interact with each other, have essential roles in ensuring normal embryonic development. In the present study, we coexpressed the human Xrcc2 and Rad51D/Rad51L3 ... proteins (Xrcc2 and Rad51D, respectively) in Escherichia coli, and purified the Xrcc2*Rad51D complex to homogeneity. The Xrcc2 small middle dotRad51D complex catalyzed homologous pairing between single-stranded and double-stranded DNA, similar to the function of the Xrcc3*Rad51C complex, which is another complex of the Rad51 paralogs. An electron microscopic analysis showed that Xrcc2*Rad51D formed a multimeric ring structure in the absence of DNA. In the presence of ssDNA, Xrcc2*Rad51D formed a filamentous structure, which is commonly observed among the human homologous pairing proteins, Rad51, Rad52, and Xrcc3*Rad51C.
Mesh Terms:
Catalysis, Circular Dichroism, Cisplatin, Cross-Linking Reagents, DNA, DNA, Single-Stranded, DNA-Binding Proteins, Dose-Response Relationship, Drug, Escherichia coli, Humans, Microscopy, Electron, Nucleoproteins, Protein Binding
Catalysis, Circular Dichroism, Cisplatin, Cross-Linking Reagents, DNA, DNA, Single-Stranded, DNA-Binding Proteins, Dose-Response Relationship, Drug, Escherichia coli, Humans, Microscopy, Electron, Nucleoproteins, Protein Binding
J. Biol. Chem.
Date: Apr. 19, 2002
PubMed ID: 11834724
View in: Pubmed Google Scholar
Download Curated Data For This Publication
216831
Switch View:
- Interactions 1