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Direct Fluorescence Monitoring of DNA Base Excision Repair

Authors :
Shenliang Wang
Eric T. Kool
Toshikazu Ono
Sheila S. David
Lisa M. Engstrom
Chi Kin Koo
Source :
Angewandte Chemie International Edition. 51:1689-1692
Publication Year :
2012
Publisher :
Wiley, 2012.

Abstract

Uracil is an undesired component of DNA, as it arises from spontaneous deamination of cytosine.[1] This hydrolysis reaction promotes mutations, since the resulting U-G pair can be misread during DNA replication. As a result, multiple cellular enzymes have evolved to detect uracil in DNA and remove it prior to replication.[2] In E. coli uracil DNA glycosylase (UDG) enzyme functions to guard the bacterial genome. In humans, similar enzyme activities exist, including the proteins UNG1/2, SMUG, and TDG.[3] These enzymes flip uracil out of the DNA helix and cleave it from its deoxyribose sugar, leaving an abasic site in its place.[4]

Details

ISSN :
14337851
Volume :
51
Database :
OpenAIRE
Journal :
Angewandte Chemie International Edition
Accession number :
edsair.doi.dedup.....65c2877de9e72533d113d808b1e81cdb
Full Text :
https://doi.org/10.1002/anie.201108135