ArticleProceedings of the National Academy of Sciences of the United States of America2008
D-loop formation by Brh2 protein of Ustilago maydis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Chromosome-Wide Characterization of Intragenic Crossover in Shiitake Mushroom,Journal of fungi (Basel, Switzerland) · 2021Article
- Dual DNA-binding domains shape the interaction of Brh2 with DNA.DNA repair · 2014Article
- Interactions between BRCA2 and RAD51 for promoting homologous recombination in Leishmania infantum.Nucleic acids research · 2012Article
- Unraveling the mechanism of BRCA2 in homologous recombination.Nature structural & molecular biology · 2011Review
- Vital roles of the second DNA-binding site of Rad52 protein in yeast homologous recombination.The Journal of biological chemistry · 2011Article
- Identification of a chemical that inhibits the mycobacterial UvrABC complex in nucleotide excision repair.Biochemistry · 2011Article
- Article
- Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination.Nature structural & molecular biology · 2010Article
- Brh2 promotes a template-switching reaction enabling recombinational bypass of lesions during DNA synthesis.Molecular cell · 2009Article
- A non-canonical DNA structure enables homologous recombination in various genetic systems.The Journal of biological chemistry · 2009Article
- Recombination activator function of the novel RAD51- and RAD51B-binding protein, human EVL.The Journal of biological chemistry · 2009Article
- DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA.The Journal of biological chemistry · 2009Article
- Second-end capture in DNA double-strand break repair promoted by Brh2 protein of Ustilago maydis.Molecular cell · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Brh2, the ortholog of the BRCA2 tumor suppressor in Ustilago maydis, works hand in hand with Rad51 to promote repair of DNA by homologous recombination. Previous studies established that Brh2 can stimulate DNA strand exchange by enabling Rad51 nucleoprotein filament formation on replication protein A-coated ssDNA. But, more recently, it was noted that Brh2 has an inherent DNA annealing activity, raising the notion that it might have roles in recombination in addition to or beyond the mediator function. Here, we found that Brh2 can autonomously promote the formation of D-loops in reactions with plasmid DNA and homologous single-stranded oligonucleotides. The reaction differs from that catalyzed by Rad51 in having no requirement for cofactors or preloading phase on ssDNA. D-loop formation was most effective when Brh2 was mixed with plasmid DNA before addition of single-stranded oligomer. D-loop formation catalyzed by Rad51 was also enhanced when Brh2 was premixed with plasmid DNA. Brh2 rendered defective in Rad51 interaction by mutation in the BRC element was still capable of promoting D-loop formation. However, the mutant protein was unable to enhance the Rad51-catalyzed reaction. The results suggest a model in which Brh2 binding to plasmid DNA attracts and helps capture Rad51-coated ssDNA.
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