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Role of polymerase β in complementing aprataxin deficiency during abasic-site base excision repair
- Source :
- Nature structuralmolecular biology. 21(5)
- Publication Year :
- 2013
-
Abstract
- DNA polymerase β (pol β) lyase removal of 5'-deoxyribose phosphate (5'-dRP) from base excision repair (BER) intermediates is critical in mammalian BER involving the abasic site. We found that pol β also removes 5'-adenylated dRP from BER intermediates after abortive ligation. The crystal structure of a human pol β-DNA complex showed the 5'-AMP-dRP group positioned in the lyase active site. Pol β expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.
- Subjects :
- Models, Molecular
DNA Repair
DNA polymerase
viruses
Crystallography, X-Ray
Article
chemistry.chemical_compound
Structural Biology
Humans
AP site
Molecular Biology
DNA Polymerase beta
Aprataxin
biology
Nuclear Proteins
Processivity
Base excision repair
DNA
Molecular biology
Protein Structure, Tertiary
DNA-Binding Proteins
Biochemistry
chemistry
biology.protein
Ligation
Nucleotide excision repair
Subjects
Details
- ISSN :
- 15459985
- Volume :
- 21
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Nature structuralmolecular biology
- Accession number :
- edsair.doi.dedup.....fc7fe468098f9f9f000ec01d05a67ca4