Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein

Tuo, Jingsheng; Chen, Catheryne; Zeng, Xianmin; Christiansen, Mette; Bohr, Vilhelm A.

doi:10.1016/s1568-7864(02)00116-7

Cited by 87 publications

(67 citation statements)

References 48 publications

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“…We show that CS-A cell extracts are not impaired in 8-OH-Gua cleavage ability, whereas extracts from CS-B cells present a reduced capacity to cleave at 8-OH-Gua residues located in oligonucleotides (Dianov et al, 1999;Tuo et al, 2001Tuo et al, , 2003. It has been hypothesized that CSB would induce transcription of genes encoding DNA glycosylases such as OGG1 (Dianov et al, 1999;Tuo et al, 2002). Suggestion of a defect in the transcriptional response of CS-B cells after H 2 O 2 treatment has been provided (Kyng et al, 2003) and a recent study demonstrates that CSB is involved in the regulation of the transcriptional program after UV damage (Proietti-De-Santis et al, 2006).…”

Section: Discussionmentioning

confidence: 86%

The role of CSA in the response to oxidative DNA damage in human cells

et al. 2007

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Cockayne syndrome (CS) is a rare genetic disease characterized by severe growth, mental retardation and pronounced cachexia. CS is most frequently due to mutations in either of two genes, CSB and CSA. Evidence for a role of CSB protein in the repair of oxidative DNA damage has been provided recently. Here, we show that CSA is also involved in the response to oxidative stress. CS-A human primary fibroblasts and keratinocytes showed hypersensitivity to potassium bromate, a specific inducer of oxidative damage. This was associated with inefficient repair of oxidatively induced DNA lesions, namely 8-hydroxyguanine (8-OH-Gua) and (5 0 S)-8,5 0 -cyclo 2 0 -deoxyadenosine. Expression of the wild-type CSA in the CS-A cell line CS3BE significantly decreased the steady-state level of 8-OH-Gua and increased its repair rate following oxidant treatment. CS-A cell extracts showed normal 8-OH-Gua cleavage activity in an in vitro assay, whereas CS-B cell extracts were confirmed to be defective. Our data provide the first in vivo evidence that CSA protein contributes to prevent accumulation of various oxidized DNA bases and underline specific functions of CSB not shared with CSA. These findings support the hypothesis that defective repair of oxidative DNA damage is involved in the clinical features of CS patients.

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Section: Discussionmentioning

confidence: 86%

The role of CSA in the response to oxidative DNA damage in human cells

et al. 2007

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“…However, the effect of ERCC6 alone is likely related to ERCC6's role as a common player in DNA metabolism (28,29). ERCC6 functions in DNA repair, regardless of whether the repair is transcription coupled or base incision, as a partner in protein complexes (30,40). It has been reported that overexpression of just one element in an enzyme complex can adversely affect the desired end result (41)(42)(43)(44)(45).…”

Section: Discussionmentioning

confidence: 99%

“…Oxidative stress induces various types of DNA damage that contribute significantly to aging and age-related disorders (26). The ERCC6 gene (alternate name CSB) plays roles in the aging process (27) and is known to function extensively in repair of damaged DNA (28)(29)(30). The disruption of ERCC6 is causal to a subtype of Cockayne syndrome, an autosomal, recessive human disorder marked by striking somatic and neurological impairment (31).…”

mentioning

confidence: 99%

Synergic effect of polymorphisms inERCC65′ flanking region andcomplement factor Hon age-related macular degeneration predisposition

Tuo

Ning²,

Bojanowski³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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This study investigates age-related macular degeneration (AMD) genetic risk factors through identification of a functional singlenucleotide polymorphism (SNP) and its disease association. We chose ERCC6 because of its roles in the aging process, DNA repair, and ocular degeneration from the gene disruption. Bioinformatics indicated a putative binding-element alteration on the sequence containing C؊6530>G SNP in the 5 flanking region of ERCC6 from Sp1 on the C allele to SP1, GATA-1, and OCT-1 on the G allele. Electrophoretic mobility shift assays displayed distinctive C and G allele-binding patterns to nuclear proteins. Luciferase expression was higher in the vector construct containing the G allele than that containing the C allele. A cohort of 460 advanced AMD cases and 269 age-matched controls was examined along with pathologically diagnosed 57 AMD and 18 age-matched non-AMD archived cases. ERCC6 C؊6530>G was associated with AMD susceptibility, both independently and through interaction with an SNP (rs380390) in the complement factor H (CFH) intron reported to be highly associated with AMD. A disease odds ratio of 23 was conferred by homozygozity for risk alleles at both ERCC6 and CFH compared with homozygozity for nonrisk alleles. Enhanced ERCC6 expression was observed in lymphocytes from healthy donors bearing ERCC6 C؊6530>G alleles. Intense immunostaining of ERCC6 was also found in AMD eyes from ERCC6 C؊6530>G carriers. The strong AMD predisposition conferred by the ERCC6 and CFH SNPs may result from biological epistasis, because ERCC6 functions in universal transcription as a component of RNA pol I transcription complex.Cockayne syndrome ͉ single nucleotide polymorphism ͉ gene regulation ͉ interaction ͉ DNA repair A ge-related macular degeneration (AMD) is a leading cause of visual impairment and blindness in Western countries among the elderly (1). AMD is a significant health problem in the United States, with a current estimate of Ϸ1.75 million persons with advanced AMD in the general population and Ϸ7.3 million people with early stages of AMD defined by large retinal drusen. By the year 2020, it is estimated that Ϸ2.95 million people will suffer advanced AMD, and an additional 6.4 million white individuals will have the early stages of AMD in at least one eye (2).The etiology of AMD remains elusive. To date, age and cigarette smoking have been identified as AMD risk factors (3-8). Various studies have indicated a significant genetic contribution to AMD risk (9). For example, it has been reported that advanced AMD is more prevalent in Caucasian populations as compared with other races that possess higher levels of uveal pigmentation and skin melanin (10). Furthermore, the population-attributed AMD risk related to genetic factors was 23% (11, 12). First-degree relatives of patients with late AMD developed the disease at an increased rate at a relatively young age (12, 13). The higher occurrence of AMD among monozygotic twins and first-degree relatives of AMD patients as compared with spouses and unrelated ...

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“…However, the precise mechanism by which CSB participates in the repair of 8-oxoG in both nuclear DNA and mtDNA is not yet known. Although CSB affects the function of hOGG1 as described above, there is no direct physical interaction between CSB and hOGG1; however, the proteins are present in the same protein complex (Tuo et al, 2002a). CSB also stimulates the expression of mtOGG1, but it has not yet been possible to demonstrate that the CSB protein is actually present in mitochondria.…”

Section: The Role Of Csb In Repair Of Oxidative Dna Damagementioning

confidence: 98%

The role of Cockayne Syndrome group B (CSB) protein in base excision repair and aging

Stevnsner

Müftüoğlu

Aamann

et al. 2008

Mechanisms of Ageing and Development

123

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Cockayne Syndrome (CS) is a rare human genetic disorder characterized by progressive multisystem degeneration and segmental premature aging. The CS complementation group B (CSB) protein is engaged in transcription coupled and global nucleotide excision repair, base excision repair and general transcription. However, the precise molecular function of the CSB protein is still unclear. In the current review we discuss the involvement of CSB in some of these processes, with focus on the role of CSB in repair of oxidative damage, as deficiencies in the repair of these lesions may be an important aspect of the premature aging phenotype of CS.

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Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein

Cited by 87 publications

References 48 publications

The role of CSA in the response to oxidative DNA damage in human cells

The role of CSA in the response to oxidative DNA damage in human cells

Synergic effect of polymorphisms inERCC65′ flanking region andcomplement factor Hon age-related macular degeneration predisposition

The role of Cockayne Syndrome group B (CSB) protein in base excision repair and aging

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