Quick Search:

uzh logo
Browse by:
bullet
bullet
bullet
bullet

Zurich Open Repository and Archive 

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-34304

Barrett, T E; Savva, R; Panayotou, G; Barlow, T; Brown, T; Jiricny, J; Pearl, L H (1998). Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell, 92(1):117-129.

[img] PDF - Registered users only
843kB

Abstract

G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
DDC:570 Life sciences; biology
Language:English
Date:1998
Deposited On:09 Jul 2010 12:54
Last Modified:15 Dec 2013 23:04
Publisher:Elsevier
ISSN:0092-8674
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1016/S0092-8674(00)80904-6
PubMed ID:9489705
Citations:Web of Science®. Times Cited: 188
Google Scholar™
Scopus®. Citation Count: 184

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page