Literature DB >> 35596054

XPG in the Nucleotide Excision Repair and Beyond: a study on the different functional aspects of XPG and its associated diseases.

Riasha Pal1, Nilanjan Paul1, Deep Bhattacharya1, Sudeshna Rakshit1, Geetha Shanmugam1, Koustav Sarkar2.   

Abstract

Several proteins are involved in DNA repair mechanisms attempting to repair damages to the DNA continuously. One such protein is Xeroderma Pigmentosum Complementation Group G (XPG), a significant component in the Nucleotide Excision Repair (NER) pathway. XPG is accountable for making the 3' incision in the NER, while XPF-ERCC4 joins ERCC1 to form the XPF-ERCC1 complex. This complex makes a 5' incision to eliminate bulky DNA lesions. XPG is also known to function as a cofactor in the Base Excision Repair (BER) pathway by increasing hNth1 activity, apart from its crucial involvement in the NER. Reports suggest that XPG also plays a non-catalytic role in the Homologous Recombination Repair (HRR) pathway by forming higher-order complexes with BRCA1, BRCA2, Rad51, and PALB2, further influencing the activity of these molecules. Studies show that, apart from its vital role in repairing DNA damages, XPG is also responsible for R-loop formation, which facilitates exhibiting phenotypes of Werner Syndrome. Though XPG has a role in several DNA repair pathways and molecular mechanisms, it is primarily a NER protein. Unrepaired and prolonged DNA damage leads to genomic instability and facilitates neurological disorders, aging, pigmentation, and cancer susceptibility. This review explores the vital role of XPG in different DNA repair mechanisms which are continuously involved in repairing these damaged sites and its failure leading to XP-G, XP-G/CS complex phenotypes, and cancer progression.
© 2022. The Author(s), under exclusive licence to Springer Nature B.V.

Entities:  

Keywords:  Base excision repair; Homologous recombination repair, R-loops; Nucleotide excision repair; Xeroderma Pigmentosum complementation group G

Mesh:

Substances:

Year:  2022        PMID: 35596054     DOI: 10.1007/s11033-022-07324-1

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.742


  63 in total

1.  Definition of a short region of XPG necessary for TFIIH interaction and stable recruitment to sites of UV damage.

Authors:  Fabrizio Thorel; Angelos Constantinou; Isabelle Dunand-Sauthier; Thierry Nouspikel; Philippe Lalle; Anja Raams; Nicolaas G J Jaspers; Wim Vermeulen; Mahmud K K Shivji; Richard D Wood; Stuart G Clarkson
Journal:  Mol Cell Biol       Date:  2004-12       Impact factor: 4.272

2.  The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity.

Authors:  Isabelle Dunand-Sauthier; Marcel Hohl; Fabrizio Thorel; Pascale Jaquier-Gubler; Stuart G Clarkson; Orlando D Schärer
Journal:  J Biol Chem       Date:  2004-12-07       Impact factor: 5.157

Review 3.  Base excision repair.

Authors:  Hans E Krokan; Magnar Bjørås
Journal:  Cold Spring Harb Perspect Biol       Date:  2013-04-01       Impact factor: 10.005

4.  The non-catalytic function of XPG protein during dual incision in human nucleotide excision repair.

Authors:  M Wakasugi; J T Reardon; A Sancar
Journal:  J Biol Chem       Date:  1997-06-20       Impact factor: 5.157

5.  Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair.

Authors:  A Constantinou; D Gunz; E Evans; P Lalle; P A Bates; R D Wood; S G Clarkson
Journal:  J Biol Chem       Date:  1999-02-26       Impact factor: 5.157

6.  Identification of the XPG region that causes the onset of Cockayne syndrome by using Xpg mutant mice generated by the cDNA-mediated knock-in method.

Authors:  Naoko Shiomi; Seiji Kito; Masaki Oyama; Tsukasa Matsunaga; Yoshi-Nobu Harada; Masahito Ikawa; Masaru Okabe; Tadahiro Shiomi
Journal:  Mol Cell Biol       Date:  2004-05       Impact factor: 4.272

Review 7.  XPG: its products and biological roles.

Authors:  Orlando D Schärer
Journal:  Adv Exp Med Biol       Date:  2008       Impact factor: 2.622

Review 8.  Flap endonuclease 1: a central component of DNA metabolism.

Authors:  Yuan Liu; Hui-I Kao; Robert A Bambara
Journal:  Annu Rev Biochem       Date:  2004       Impact factor: 23.643

9.  Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.

Authors:  Michał Miętus; Elżbieta Nowak; Marcin Jaciuk; Paweł Kustosz; Justyna Studnicka; Marcin Nowotny
Journal:  Nucleic Acids Res       Date:  2014-08-12       Impact factor: 16.971

10.  The involvement of nucleotide excision repair proteins in the removal of oxidative DNA damage.

Authors:  Namrata Kumar; Sripriya Raja; Bennett Van Houten
Journal:  Nucleic Acids Res       Date:  2020-11-18       Impact factor: 16.971

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