Chaperones for dancing on chromatin: Role of post‐translational modifications in dynamic damage detection hand‐offs during nucleotide excision repair

Houten, Bennett Van; Schnable, Brittani L; Kumar, Namrata

doi:10.1002/bies.202100011

Cited by 3 publications

(2 citation statements)

References 48 publications

(66 reference statements)

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“…Alternatively, in the GG-NER pathway, most lesions are recognized by a multiprotein complex that contains XP group C-complementing protein (XPC), radiation sensitive 23B (RAD23B), and Centrin 2 (CETN2) [62]. However, UV-induced pyrimidine dimers are more readily recognized by the UV-DDB complex that recruits XPC, where DDB2 binds to the damaged site and flips two bases into the recognition pocket [63,64]. DDB1 functions as a substrate for the E3 ubiquitin ligase complex CUL4-RBX1 that can ubiquitylate DDB2 and XPC [65].…”

Section: Nucleotide Excision Repair (Ner)mentioning

confidence: 99%

New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways

Waters,

Spratt

2024

IJMS

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Maintaining genomic stability and properly repairing damaged DNA is essential to staying healthy and preserving cellular homeostasis. The five major pathways involved in repairing eukaryotic DNA include base excision repair (BER), nucleotide excision repair (NER), mismatch repair (MMR), non-homologous end joining (NHEJ), and homologous recombination (HR). When these pathways do not properly repair damaged DNA, genomic stability is compromised and can contribute to diseases such as cancer. It is essential that the causes of DNA damage and the consequent repair pathways are fully understood, yet the initial recruitment and regulation of DNA damage response proteins remains unclear. In this review, the causes of DNA damage, the various mechanisms of DNA damage repair, and the current research regarding the early steps of each major pathway were investigated.

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Section: Nucleotide Excision Repair (Ner)mentioning

confidence: 99%

New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways

Waters,

Spratt

2024

IJMS

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“…NER consists of two distinct sub-pathways, global genome NER (GG-NER) and transcription-coupled NER (TC-NER), which are the main pathways used to remove massive DNA damage in mammals [ 23 ]. GG-NER repairs DNA damage both in transcribed and non-transcribed DNA strands.…”

Section: The Role Of Ddb2 In Nermentioning

confidence: 99%

A protein with broad functions: damage-specific DNA-binding protein 2

2022

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Damage-specific DNA-binding protein 2 (DDB2) was initially identified as a component of the damage-specific DNA-binding heterodimeric complex, which cooperates with other proteins to repair UV-induced DNA damage. DDB2 is involved in the occurrence and development of cancer by affecting nucleotide excision repair (NER), cell apoptosis, and premature senescence. DDB2 also affects the sensitivity of cancer cells to radiotherapy and chemotherapy. In addition, a recent study found that DDB2 is a pathogenic gene for hepatitis and encephalitis. In recent years, there have been few relevant literature reports on DDB2, so there is still room for further research about it. In this paper, the molecular mechanisms of different biological processes involving DDB2 are reviewed in detail to provide theoretical support for research on drugs that can target DDB2.

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The role of UV-DDB in processing 8-oxoguanine during base excision repair

Nagpal

Raja

Houten

2022

Biochemical Society Transactions

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Recent data from our laboratory has shown that the nucleotide excision repair (NER) proteins UV-damaged DNA-binding protein (UV-DDB), xeroderma pigmentosum group C (XPC), and xeroderma pigmentosum group A (XPA) play important roles in the processing of 8-oxoG. This review first discusses biochemical studies demonstrating how UV-DDB stimulates human 8-oxoG glycosylase (OGG1), MUTYH, and apurinic/apyrimidinic (AP) endonuclease (APE1) to increase their turnover at damage sites. We further discuss our single-molecule studies showing that UV-DDB associates with these proteins at abasic moieties on DNA damage arrays. Data from cell experiments are then described showing that UV-DDB interacts with OGG1 at sites of 8-oxoG. Finally, since many glycosylases are inhibited from working on damage in the context of chromatin, we present a working model of how UV-DDB may be the first responder to alter the structure of damage containing-nucleosomes to allow access by base excision repair (BER) enzymes.

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Chaperones for dancing on chromatin: Role of post‐translational modifications in dynamic damage detection hand‐offs during nucleotide excision repair

Cited by 3 publications

References 48 publications

New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways

New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways

A protein with broad functions: damage-specific DNA-binding protein 2

The role of UV-DDB in processing 8-oxoguanine during base excision repair

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