Ask about this productRelated genes to: RAD51 antibody
- Gene:
- RAD51 NIH gene
- Name:
- RAD51 recombinase
- Previous symbol:
- RAD51A, RECA
- Synonyms:
- HsRad51, HsT16930, BRCC5, FANCR
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-05-26
- Date modifiied:
- 2017-05-02
- Gene:
- RAD51B NIH gene
- Name:
- RAD51 paralog B
- Previous symbol:
- RAD51L1
- Synonyms:
- REC2, hREC2, R51H2
- Chromosome:
- 14q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-09-12
- Date modifiied:
- 2016-10-05
- Gene:
- RAD51C NIH gene
- Name:
- RAD51 paralog C
- Previous symbol:
- -
- Synonyms:
- RAD51L2, FANCO
- Chromosome:
- 17q22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-26
- Date modifiied:
- 2019-04-23
- Gene:
- RAD51D NIH gene
- Name:
- RAD51 paralog D
- Previous symbol:
- RAD51L3
- Synonyms:
- R51H3, Trad, HsTRAD
- Chromosome:
- 17q12
- Locus Type:
- gene with protein product
- Date approved:
- 1998-05-27
- Date modifiied:
- 2019-04-23
Related products to: RAD51 antibody
Related articles to: RAD51 antibody
- The repair of DNA double-strand breaks by homologous recombination is essential for genomic integrity, and its dysregulation is a hallmark of cancer. Central to homologous recombination is the RAD51 recombinase, whose assembly into a nucleoprotein filament is governed by five RAD51 paralogues (RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3). Mutations in any of these proteins predispose individuals to multiple cancers or genetic disorders. These paralogues are thought to form two functionally separate complexes RAD51B-RAD51C-RAD51D-XRCC2 (BCDX2) and RAD51C-XRCC3 (CX3), that act independently at different stages of homologous recombination. Here we demonstrate that all five paralogues can assemble into a single, ATP-dependent BCDX2-CX3-RAD51 supercomplex. The architecture of this assembly bound to single-stranded DNA reveals a contiguous filament where the CX3 module stacks atop BCDX2, creating a protofilament template for RAD51 filament formation. We further identify a novel, RAD51B-independent DX2-CX3 complex (RAD51D-XRCC2-RAD51C-XRCC3) functioning as a stable RAD51 anchor on single-stranded DNA, and we capture it in multiple states, including capping RAD51 filament segment. These distinct assemblies are differentially regulated by ATPase activity, defining a dynamic BCDX2-CX3 'loader' and a stable DX2-CX3 'anchor' that provide functional modularity to the homologous recombination machinery. This work provides a unifying mechanism for human RAD51 paralogue function and delivers an atomic blueprint for interpreting disease-causing mutations. - Source: PubMed
Publication date: 2026/03/02
Koo Christopher WXiao JiaqiCoassolo SebastienLiu JieYu ChristineAzumaya Caleigh MGore Steven KCheung Tommy KBrillantes BobbyRose Christopher MHeyer Wolf-DietrichCiferri ClaudioYatskevich Stanislau - Double-strand break (DSB) repair occurs through non-homologous end joining (NHEJ) or homologous recombination (HR). To identify non-canonical factors that influence DSB repair outcomes, we parsed data from pooled genetic screens. Through this approach, we identified the splicing factor SFPQ, which has been previously reported to associate with DSBs and promote repair. Here, we show that SFPQ depletion alters DSB repair via HR. However, in contrast to other published work, we find that SFPQ does not localize to DSBs but instead stabilizes the expression of RAD51 and its paralogs independently of p53 activation or DNA damage. Our findings suggest that SFPQ contributes to constitutive DSB repair by maintaining RAD51 paralog mRNA stability rather than through direct interaction with DSBs or RAD51 proteins. Ultimately, our results highlight indirect mechanisms by which RNA-binding proteins can influence genome stability. - Source: PubMed
Publication date: 2026/02/10
Gotthold SofiaHansen Keile RBrown Andrew NChowdhury Soham PJoyce Christine MVinish VirajRodriguez Sofie IJain SambhavGhasemi Hannah IYoon Amanda CBacal JulienMorrissey Meghan AGardner Brooke MRichardson Chris D - Homologous recombination repairs DNA double-strand breaks and protects stalled replication forks, but how the five RAD51 paralogs contribute to these processes remains unclear. Mutations in the RAD51 paralogs are linked to heritable breast and ovarian cancers and the cancer-prone disease Fanconi anemia. In this work, we show that the RAD51 paralogs assemble into two distinct heterotetrameric complexes, RAD51B-RAD51C-RAD51D-XRCC2 (RAD51B complex) and XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex). The RAD51B complex promotes dynamic adenosine triphosphate hydrolysis-dependent assembly of RAD51 filaments, whereas the XRCC3 complex stably caps the 5' termini of RAD51 filaments to promote homologous pairing, as visualized by cryo-electron microscopy. Highly conserved across evolution, the XRCC3 complex reveals insights into RAD51 filament formation and capping during DNA repair and replication fork stabilization. - Source: PubMed
Publication date: 2026/02/26
Greenhough Luke AGalanti LorenzoLiang Chih-ChaoBoulton Simon JWest Stephen C - Double-strand break (DSB) repair occurs through non-homologous end joining (NHEJ) or homologous recombination (HR). To identify non-canonical factors that influence DSB repair outcomes, we parsed data from pooled genetic screens. Through this approach, we identified the splicing factor SFPQ, which has been previously reported to associate with DSBs and promote repair. Here, we show that SFPQ depletion alters DSB repair via HR. However, in contrast to other published work, we find that SFPQ does not localize to DSBs but instead stabilizes the expression of RAD51 and its paralogs independently of p53 activation or DNA damage. Our findings suggest that SFPQ contributes to constitutive DSB repair by maintaining RAD51 paralog mRNA stability rather than through direct interaction with DSBs or RAD51 protein and highlight indirect mechanisms by which RNA-binding proteins can influence genome stability. - Source: PubMed
Publication date: 2025/09/08
Gotthold SofiaHansen Keile RBrown Andrew NChowdhury Soham PGhasemi Hannah IYoon Amanda CJoyce Christine MBacal JulienGardner Brooke MRichardson Chris D - Esophageal adenocarcinoma (EAC) remains a devastating disease and second line treatment options in the metastatic space are limited. Homologous recombination (HR) defects have been described in EAC in up to 40% of patients. Poly (ADP-ribose) polymerase (PARP)1 and PARP2 inhibitors have shown efficacy in HR defective prostate and ovarian cancers. Here, we describe the activity of the PARP inhibitor niraparib in metastatic EAC with HR defects. - Source: PubMed
Publication date: 2024/11/21
Khalid Ahmed BilalFountzilas ChristosBurney Heather NMamdani HirvaSchneider Bryan PFausel ChristopherPerkins Susan MJalal Shadia