ArticleThe Journal of biological chemistry2009
DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Moss BRCA2 lacking the canonical DNA-binding domain promotes homologous recombination and binds to DNA.Nucleic acids research · 2025Article
- Exploring the structural landscape of DNA maintenance proteins.Nature communications · 2024Article
- Visualization of direct and diffusion-assisted RAD51 nucleation by full-length human BRCA2 protein.Molecular cell · 2023Article
- Missense Variants of Uncertain Significance: A Powerful Genetic Tool for Function Discovery with Clinical Implications.Cancers · 2021Review
- Collaboration in the actions of Brh2 with resolving functions during DNA repair and replication stress in Ustilago maydis.DNA repair · 2018Article
- Dss1 Regulates Association of Brh2 with Rad51.Biochemistry · 2017Article
- Distinct binding of BRCA2 BRC repeats to RAD51 generates differential DNA damage sensitivity.Nucleic acids research · 2016Article
- Promotion of BRCA2-Dependent Homologous Recombination by DSS1 via RPA Targeting and DNA Mimicry.Molecular cell · 2015Article
- Dual DNA-binding domains shape the interaction of Brh2 with DNA.DNA repair · 2014Article
- Dss1 release activates DNA binding potential in Brh2.Biochemistry · 2012Article
- Brh2 domain function distinguished by differential cellular responses to DNA damage and replication stress.Molecular microbiology · 2012Article
- Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Plasticity of BRCA2 function in homologous recombination: genetic interactions of the PALB2 and DNA binding domains.PLoS genetics · 2011Article
- Unraveling the mechanism of BRCA2 in homologous recombination.Nature structural & molecular biology · 2011Review
- Mutational analysis of Brh2 reveals requirements for compensating mediator functions.Molecular microbiology · 2011Article
- Overexpression of RAD51 suppresses recombination defects: a possible mechanism to reverse genomic instability.Nucleic acids research · 2010Review
- Dss1 regulates interaction of Brh2 with DNA.Biochemistry · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The C-terminal region of Brh2 (Brh2(CT)), the BRCA2 homolog in Ustilago maydis, is highly conserved and aligns with the DSS1/DNA-binding domain (DBD) of mammalian BRCA2, while the N-terminal region (Brh2(NT)) is poorly conserved and has no obvious functional domain except for the single Rad51-interacting BRC element. Paradoxically, Brh2(NT), but not Brh2(CT), complements the DNA repair and recombination deficiency of the brh2 mutant. We show here that Brh2(NT) exhibits an unexpected DNA binding activity with properties similar to that of the full-length protein. Deletion mapping localized the region responsible for the DNA binding activity to a stretch of residues between the BRC element and the canonical DBD. A heterologous DNA-binding domain from the large subunit of replication protein A substituted for the endogenous binding region within Brh2(NT) in supporting DNA repair. Rad51-promoted strand invasion was stimulated by Brh2(NT), but required the presence of the BRC element. The findings suggest a model in which Brh2(NT) serves as the principal site for association with DNA, while the Brh2(CT) provides a means for regulation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.