RAD51-associated protein 1

Definition:

Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination. Key mediator of alternative lengthening of telomeres (ALT) pathway, a homology-directed repair mechanism of telomere elongation that controls proliferation in aggressive cancers, by stimulating homologous recombination. May also bind RNA; additional evidences are however required to confirm RNA-binding in vivo.

References:

[1]. Ann C Parplys, et al. RAD51AP1-deficiency in vertebrate cells impairs DNA replication. DNA Repair (Amst). 2014 Dec;24:87-97. [Content Brief]

[2]. Eloïse Dray, et al. Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2. Nat Struct Mol Biol. 2010 Oct;17(10):1255-9. [Content Brief]

[3]. Fengshan Liang, et al. Promotion of RAD51-Mediated Homologous DNA Pairing by the RAD51AP1-UAF1 Complex. Cell Rep. 2016 Jun 7;15(10):2118-2126. [Content Brief]

[4]. Jonathan Barroso-González, et al. RAD51AP1 Is an Essential Mediator of Alternative Lengthening of Telomeres. Mol Cell. 2019 Oct 3;76(1):11-26.e7. [Content Brief]

[5]. Scott Cukras, et al. The USP1-UAF1 complex interacts with RAD51AP1 to promote homologous recombination repair. Cell Cycle. 2016 Oct;15(19):2636-2646. [Content Brief]

[6]. O V Kovalenko, et al. A novel nucleic acid-binding protein that interacts with human rad51 recombinase. Nucleic Acids Res. 1997 Dec 15;25(24):4946-53. [Content Brief]

[7]. Myun Hwa Dunlop, et al. Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair. J Biol Chem. 2012 Apr 6;287(15):12343-7. [Content Brief]

[8]. Claudia Wiese, et al. Promotion of homologous recombination and genomic stability by RAD51AP1 via RAD51 recombinase enhancement. Mol Cell. 2007 Nov 9;28(3):482-90. [Content Brief]

[9]. Ann C Parplys, et al. NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability. Nucleic Acids Res. 2015 Nov 16;43(20):9817-34. [Content Brief]

[10]. Fengshan Liang, et al. DNA requirement in FANCD2 deubiquitination by USP1-UAF1-RAD51AP1 in the Fanconi anemia DNA damage response. Nat Commun. 2019 Jun 28;10(1):2849. [Content Brief]

[11]. Eloïse Dray, et al. Molecular basis for enhancement of the meiotic DMC1 recombinase by RAD51 associated protein 1 (RAD51AP1). Proc Natl Acad Sci U S A. 2011 Mar 1;108(9):3560-5. [Content Brief]

[12]. Mauro Modesti, et al. RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. Mol Cell. 2007 Nov 9;28(3):468-81. [Content Brief]

[13]. Fengshan Liang, et al. The DNA-binding activity of USP1-associated factor 1 is required for efficient RAD51-mediated homologous DNA pairing and homology-directed DNA repair. J Biol Chem. 2020 Jun 12;295(24):8186-8194. [Content Brief]

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