Replication protein A 32 kDa subunit

Definition:

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.

References:

[1]. Zihua Gong, et al. E3 ligase RFWD3 participates in replication checkpoint control. J Biol Chem. 2011 Jun 24;286(25):22308-13. [Content Brief]

[2]. M S DeMott, et al. Replication protein A stimulates long patch DNA base excision repair. J Biol Chem. 1998 Oct 16;273(42):27492-8. [Content Brief]

[3]. L F Erdile, et al. The primary structure of the 32-kDa subunit of human replication protein A. J Biol Chem. 1990 Feb 25;265(6):3177-82. [Content Brief]

[4]. Z He, et al. RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature. 1995 Apr 6;374(6522):566-9. [Content Brief]

[5]. A Aboussekhra, et al. Mammalian DNA nucleotide excision repair reconstituted with purified protein components. Cell. 1995 Mar 24;80(6):859-68. [Content Brief]

[6]. Aaron C Mason, et al. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. [Content Brief]

[7]. Klaus Weisshart, et al. Coordinated regulation of replication protein A activities by its subunits p14 and p32. J Biol Chem. 2004 Aug 20;279(34):35368-76. [Content Brief]

[8]. Dong-Hyun Lee, et al. A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat Struct Mol Biol. 2010 Mar;17(3):365-72. [Content Brief]

[9]. M S Park, et al. Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells. J Biol Chem. 1996 Aug 2;271(31):18996-9000. [Content Brief]

[10]. Kate M Sleeth, et al. RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells. J Mol Biol. 2007 Oct 12;373(1):38-47. [Content Brief]

[11]. Alexandre Maréchal, et al. PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry. Mol Cell. 2014 Jan 23;53(2):235-246. [Content Brief]

[12]. Amra Grudic, et al. Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres. Nucleic Acids Res. 2007;35(21):7267-78. [Content Brief]

[13]. Y L Lin, et al. The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair. J Biol Chem. 1998 Jan 16;273(3):1453-61. [Content Brief]

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