Human Base Excision Repair Creates a Bias Toward −1 Frameshift Mutations
نویسندگان
چکیده
منابع مشابه
Overexpression of DNA polymerase beta results in an increased rate of frameshift mutations during base excision repair.
DNA polymerase beta (Pol beta) is important for the base excision repair (BER) pathway. Overexpression of Pol beta is frequently found in cancer cells and is thought to be associated with tumorigenesis. In this study, we examined BER fidelity in extracts derived from a human lymphoblastoid cell line that over expresses Pol beta compared to normal control cells. Using an in vitro mutagenesis ass...
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Oxidized DNA base lesions, such as thymine glycol (Tg) and 8-hydroxyguanine, are often toxic and mutagenic and have been implicated in carcinogenesis. To clarify whether NEIL1 protein, which exhibits excision repair activity towards such base lesions, is involved in gastric carcinogenesis, we examined 71 primary gastric cancers from Japanese patients and four gastric cancer cell lines for mutat...
متن کاملInvolvement of flap endonuclease 1 in base excision DNA repair.
Base excision repair can proceed in either one of two alternative pathways: a DNA polymerase beta-dependent pathway and a proliferating cell nuclear antigen (PCNA)-dependent pathway. Excision of an apurinic/apyrimidinic (AP) site by cutting the phosphate backbone on its 3' side following incision at its 5' side by AP endonuclease is a prerequisite to completion of these repair pathways. Using a...
متن کاملThe presence of a truncated base excision repair pathway in human spermatozoa , mediated by OGG 1
DNA repair has long been considered impossible in human spermatozoa due to the high level of DNA compaction observed in these cells. However, detailed examination of the base excision repair pathway in human spermatozoa has revealed the presence of an enzyme critical to this pathway, OGG1. This glycosylase was associated with the sperm nucleus and mitochondria and could actively excise 8-hydrdo...
متن کاملHuman Base Excision Repair for Preservation of Genomic Stability
Nuclear uracil-DNA glycosylase UNG2 has anestablished role in repair of U/A pairs resulting frommisincorporation of dUMP during replication. In anti-gen-stimulated B-lymphocytes UNG2 removes uracilfrom U/G mispairs as part of somatic hypermutationand class switch recombination processes. Usingantibodies specific for the N-terminal non-catalyticdomain of UNG2, we isol...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.118596