Biochemistry (Moscow)

, Volume 76, Issue 1, pp 4–15

Role of nucleotide excision repair proteins in oxidative DNA damage repair: an updating

  • B. Pascucci
  • M. D’Errico
  • E. Parlanti
  • S. Giovannini
  • E. Dogliotti
Review

DOI: 10.1134/S0006297911010032

Cite this article as:
Pascucci, B., D’Errico, M., Parlanti, E. et al. Biochemistry Moscow (2011) 76: 4. doi:10.1134/S0006297911010032

Abstract

DNA repair is a crucial factor in maintaining a low steady-state level of oxidative DNA damage. Base excision repair (BER) has an important role in preventing the deleterious effects of oxidative DNA damage, but recent evidence points to the involvement of several repair pathways in this process. Oxidative damage may arise from endogenous and exogenous sources and may target nuclear and mitochondrial DNA as well as RNA and proteins. The importance of preventing mutations associated with oxidative damage is shown by a direct association between defects in BER (i.e. MYH DNA glycosylase) and colorectal cancer, but it is becoming increasingly evident that damage by highly reactive oxygen species plays also central roles in aging and neurodegeneration. Mutations in genes of the nucleotide excision repair (NER) pathway are associated with diseases, such as xeroderma pigmentosum and Cockayne syndrome, that involve increased skin cancer risk and/or developmental and neurological symptoms. In this review we will provide an updating of the current evidence on the involvement of NER factors in the control of oxidative DNA damage and will attempt to address the issue of whether this unexpected role may unlock the difficult puzzle of the pathogenesis of these syndromes.

Key words

oxidative damageDNA repairoxidative metabolismxeroderma pigmentosumCockayne syndrome

Abbreviations

AAF

acetylaminofluorene

Abl-1

Abelson murine leukemia kinase

AOA1

ataxia oculomotor apraxia type 1

APE1

apurinic/apyrimidinic endonuclease 1

ATR

ataxia telangiectasia and Rad 3 related

BER

base excision repair

BPDE

benzo(a)pyrene diol epoxide

CS

Cockayne syndrome

CSN

COP9 signalosome

cyPudN

8,5′-cyclopurine 2′-deoxynucleosides

DDB

DNA damage-binding protein

DRC

damage repair capacity

DSBs

double-strand DNA breaks

ES

embryonic stem

FapyA

formamide pyrimidine adenine

FapyG

formamide pyrimidine guanine

FPG

formamidopyrimidine DNA glycosylase

GGR

global genome repair

HCR

host cell reactivation

HMGN1

high-mobility group nucleosome binding domain 1

HNE

4-hydroxy-2-nonenal-modified protein

MEF

mouse embryo fibroblasts

mtSSBP-1

mitochondrial single stranded DNA binding protein

NEIL1

nei endonuclease VIII-like 1

NER

nucleotide excision repair

OGG1

8-oxoguanine DNA glycosylase

8-oxoA

8-OH-adenine

8-oxoG

8-OH-guanine

PARP-1

poly(ADP-ribose) polymerase 1

PCNA

proliferating cell nuclear antigen

PGBD3

PiggyBac transposable element-derived protein 3

RNAPII

RNA polymerase II

ROS

reactive oxygen species

RPA

replication protein A

SCAN1

spinocerebellar ataxia with axonal neuropathy

SIRT1

sirtuin 1

SMUG1

single-strand-specific monofunctional uracil-DNA glycosylases

SNP

single nucleotide polymorphisms

SOD

superoxide dismutase

SSBs

single-strand DNA breaks

TCR

transcription-coupled repair

TDG

thymine DNA glycosylase

TFIIH

transcription factor H-II

TFIIS

transcription factor S-II

Tg

thymine glycol

TGD

transglutaminase-homology domain

UVSS

UV sensitive syndrome

XAB2

XPA binding protein 2

XP

xeroderma pigmentosum

Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • B. Pascucci
    • 1
    • 2
  • M. D’Errico
    • 2
  • E. Parlanti
    • 2
  • S. Giovannini
    • 2
  • E. Dogliotti
    • 2
  1. 1.Istituto di CristallografiaConsiglio Nazionale delle RicercheMonterotondo Stazione, RomeItaly
  2. 2.Department of Environment and Primary PreventionIstituto Superiore di SanitàRomeItaly