Back to Search
Start Over
Defective repair of 5-hydroxy-2′-deoxycytidine in Cockayne syndrome cells and its complementation by Escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III
- Source :
- Free Radical Biology and Medicine. 48:681-690
- Publication Year :
- 2010
- Publisher :
- Elsevier BV, 2010.
-
Abstract
- Repair of the oxidized purine 8-oxo-7,8-dihydro-2'-deoxyguanosine is inefficient in cells belonging to both complementation groups A and B of Cockayne syndrome (CS), a developmental and neurological disorder characterized by defective transcription-coupled repair. We show here that both CS-A and CS-B cells are also defective in the repair of 5-hydroxy-2'-deoxycytidine (5-OHdC), an oxidized pyrimidine with cytotoxic and mutagenic properties. The defect in the repair of oxidatively damaged DNA in CS cells thus extends to oxidized pyrimidines, indicating a general flaw in the repair of oxidized lesions in this syndrome. The defect could not be reproduced in in vitro repair experiments on oligonucleotide substrates, suggesting a role for both CS-A and CS-B proteins in chromatin remodeling during 5-OHdC repair. Expression of Escherichia coli formamidopyrimidine DNA glycosylase (FPG) or endonuclease III complemented the 5-OHdC repair deficiency. Hence, the expression of a single enzyme, FPG from E. coli, stably corrects the delayed removal of both oxidized purines and oxidized pyrimidines in CS cells.
- Subjects :
- Male
Purine
Adolescent
Biology
Transfection
Deoxycytidine
Biochemistry
Chromatin remodeling
Cockayne syndrome
Deoxyribonuclease (Pyrimidine Dimer)
chemistry.chemical_compound
Physiology (medical)
Escherichia coli
medicine
Humans
Deoxyguanosine
Cockayne Syndrome
Cell Line, Transformed
Aged, 80 and over
Escherichia coli Proteins
Formamidopyrimidine DNA glycosylase
Chromatin Assembly and Disassembly
medicine.disease
DNA Repair-Deficiency Disorders
Molecular biology
Complementation
DNA-Formamidopyrimidine Glycosylase
chemistry
Child, Preschool
Female
DNA
Nucleotide excision repair
Subjects
Details
- ISSN :
- 08915849
- Volume :
- 48
- Database :
- OpenAIRE
- Journal :
- Free Radical Biology and Medicine
- Accession number :
- edsair.doi.dedup.....36eb0c26e21c857b5e54de5aae21d08b