DNA excision repair protein ERCC-5

Definition:

Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble. Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA. Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II. Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity. Required for DNA replication fork maintenance and preservation of genomic stability. Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site. During HRR, binds to the replication fork with high specificity and stabilizes it. Also, acts upstream of HRR, to promote the release of BRCA1 from DNA.

References:

[1]. K G Cloud, et al. XPG protein has a structure-specific endonuclease activity. Mutat Res. 1995 Jul;347(2):55-60. [Content Brief]

[2]. Y Habraken, et al. Human xeroderma pigmentosum group G gene encodes a DNA endonuclease. Nucleic Acids Res. 1994 Aug 25;22(16):3312-6. [Content Brief]

[3]. A O'Donovan, et al. XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair. Nature. 1994 Sep 29;371(6496):432-5. [Content Brief]

[4]. A O'Donovan, et al. Isolation of active recombinant XPG protein, a human DNA repair endonuclease. J Biol Chem. 1994 Jun 10;269(23):15965-8. [Content Brief]

[5]. Kelly S Trego, et al. Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologous Recombination and Genome Stability. Mol Cell. 2016 Feb 18;61(4):535-546. [Content Brief]

[6]. T Bessho, et al. Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. Nucleic Acids Res. 1999 Feb 15;27(4):979-83. [Content Brief]

[7]. Altaf H Sarker, et al. Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome. Mol Cell. 2005 Oct 28;20(2):187-98. [Content Brief]

[8]. Susan E Tsutakawa, et al. Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations. Proc Natl Acad Sci U S A. 2020 Jun 23;117(25):14127-14138. [Content Brief]

[9]. Rocío González-Corrochano, et al. The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair. Nucleic Acids Res. 2020 Sep 25;48(17):9943-9958. [Content Brief]

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