Repair of dihydrouracil supported by base excision repair in mNTH1 knock-out cell extracts.

2.50
Hdl Handle:
http://hdl.handle.net/10541/83548
Title:
Repair of dihydrouracil supported by base excision repair in mNTH1 knock-out cell extracts.
Authors:
Elder, Rhoderick H; Dianov, Grigory L
Abstract:
In mammalian cells, thymine glycols and other oxidized pyrimidines such as 5,6-dihydrouracil are removed from DNA by the NTH1 protein, a bifunctional DNA-N-glycosylase. However, mNTH1 knock-out mice in common with other DNA glycosylase-deficient mice do not show any severe abnormalities associated with accumulation of DNA damage and mutations. In the present study we used an in vitro repair system to investigate the mechanism for the removal of 5,6-dihydrouracil from DNA by mNTH1-deficient cell-free extracts derived from testes of mNTH1 knock-out mice. We found that these extracts are able to support the removal of 5,6-dihydrouracil from DNA at about 20% of the efficiency of normal extracts. Furthermore, we also found that single-nucleotide patch base excision repair is the major pathway for removal of 5,6-dihydrouracil in mNTH1-deficient cell extracts, suggesting the involvement of other DNA glycosylase(s) in the removal of oxidized pyrimidines.
Affiliation:
Medical Research Council Radiation and Genome Stability Unit, Harwell, Oxfordshire, OX11 0RD, United Kingdom.
Citation:
Repair of dihydrouracil supported by base excision repair in mNTH1 knock-out cell extracts. 2002, 277 (52):50487-90 J. Biol. Chem.
Journal:
The Journal of Biological Chemistry
Issue Date:
27-Dec-2002
URI:
http://hdl.handle.net/10541/83548
DOI:
10.1074/jbc.M208153200
PubMed ID:
12401779
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorElder, Rhoderick H-
dc.contributor.authorDianov, Grigory L-
dc.date.accessioned2009-10-05T15:43:21Z-
dc.date.available2009-10-05T15:43:21Z-
dc.date.issued2002-12-27-
dc.identifier.citationRepair of dihydrouracil supported by base excision repair in mNTH1 knock-out cell extracts. 2002, 277 (52):50487-90 J. Biol. Chem.en
dc.identifier.issn0021-9258-
dc.identifier.pmid12401779-
dc.identifier.doi10.1074/jbc.M208153200-
dc.identifier.urihttp://hdl.handle.net/10541/83548-
dc.description.abstractIn mammalian cells, thymine glycols and other oxidized pyrimidines such as 5,6-dihydrouracil are removed from DNA by the NTH1 protein, a bifunctional DNA-N-glycosylase. However, mNTH1 knock-out mice in common with other DNA glycosylase-deficient mice do not show any severe abnormalities associated with accumulation of DNA damage and mutations. In the present study we used an in vitro repair system to investigate the mechanism for the removal of 5,6-dihydrouracil from DNA by mNTH1-deficient cell-free extracts derived from testes of mNTH1 knock-out mice. We found that these extracts are able to support the removal of 5,6-dihydrouracil from DNA at about 20% of the efficiency of normal extracts. Furthermore, we also found that single-nucleotide patch base excision repair is the major pathway for removal of 5,6-dihydrouracil in mNTH1-deficient cell extracts, suggesting the involvement of other DNA glycosylase(s) in the removal of oxidized pyrimidines.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshBase Sequence-
dc.subject.meshCell-Free System-
dc.subject.meshDNA Damage-
dc.subject.meshDNA Glycosylases-
dc.subject.meshDNA Repair-
dc.subject.meshDeoxyribonuclease (Pyrimidine Dimer)-
dc.subject.meshEndodeoxyribonucleases-
dc.subject.meshEscherichia coli Proteins-
dc.subject.meshMice-
dc.subject.meshMice, Knockout-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshMutation-
dc.subject.meshN-Glycosyl Hydrolases-
dc.subject.meshOligodeoxyribonucleotides-
dc.subject.meshRecombinant Proteins-
dc.subject.meshUracil-
dc.titleRepair of dihydrouracil supported by base excision repair in mNTH1 knock-out cell extracts.en
dc.typeArticleen
dc.contributor.departmentMedical Research Council Radiation and Genome Stability Unit, Harwell, Oxfordshire, OX11 0RD, United Kingdom.en
dc.identifier.journalThe Journal of Biological Chemistryen

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