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Nucleotide excision repair (NER) repairs damage to a nucleotide strand containing at least 2 bases and creating a structural distortion of the DNA. NER acts to repair single strand breaks in addition to serial damage from exogenous sources such as bulky DNA adducts and UV radiation. 26 The same pathway may be used to repair damage from oxidative stress. 27 Over 20 proteins are involved in the NER pathway in mammalian cells, including XPA, XPC-hHR23B, replication protein A (RPA), transcription factor TFIIH, XPB and XPD DNA helicases, ERCC1-XPF and XPG, Pold, Pole, PCNA, and replication factor C. 28 Overexpression of the excision repair cross-complementing.
In human cells, HR proteins include members of the MRN complex, which consist of meiotic recombination 11 (MRE11)/radiation-sensitive mutant 50 (Rad50)/Nijmegen breakage syndrome 1 (NBS1) as well as Rad51, the Rad51 paralogs (Rad51B, Rad51C, Rad51D, X-ray repair cross-complementing group 2 (XRCC2), and XRCC3), Rad54, and Rad54B . Proteins involved in the NHEJ pathway include Ku70/80, the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), ligase IV (Lig4), XRCC4 and Artemis .
The original method was by transfer of fragments of the human genome to ultraviolet light (UV)-sensitive mutant cell lines derived from Chinese hamster ovary cells.  Reflecting this cross-species genetic complementation method, the gene was called “Excision repair cross-complementing 1”. Multiple independent complementation groups of Chinese hamster ovary (CHO) cells were isolated, and this gene restored UV resistance to cells of complementation group 1.
Boboila C, Oksenych V, Gostissa M, Wang JH, Zha S, Zhang Y, Chai H, Lee CS, Jankovic M, Saez LM, et al. : Robust chromosomal DNA repair via alternative end-joining in the absence of X-ray repair cross-complementing protein 1 (XRCC1). Proc Natl Acad Sci USA 2012, 109:2473-2478. PubMed Abstract | Publisher Full Text | PubMed Central Full Text.
5 110q0 147 -192 147h-45z"> , and p53 [70, 71]. Poly(ADP-ribose) glycohydrolase (PARG) is the main enzyme involved in catabolism of poly(ADP-ribose), cleaving it into free ADP-ribose monomers . PARP-1 itself is also known to be part of chromatin structure and involved in maintaining a compact chromatin structure, preventing inadvertent transcription from occurring . Unfolding of the compact chromatin structure allows DNA regulatory and repair processes access to the damaged sites as well as to replication and transcription initiation sites . PARP-1 has been reported to play a key role in the nucleotide excision repair (NER) pathway used to remove bulky DNA adducts  and in the base excision repair (BER) pathway by interacting with BER protein XRCC1 (X-ray repair cross-complementing.
Repair of a single strand break in DNA is initiated by the binding of PARP1. PARP1 binds single-strand breaks and pulls base excision repair intermediates close, leading to the synthesis of poly-ADP ribose. XRCC1 is the X-ray repair cross complementing protein 1. XRCC1 complexes with polynucleotide kinase (PNK) which processes DNA termini. PCNA is the proliferating cell nuclear antigen that serves as a DNA clamp that aids in the DNA polymerase activity (DNA pol) FEN1 (Flap endonuclease 1) is then recruited to remove the overhanging 5' flap.