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Recent progress in the biology, chemistry and structural biology of DNA glycosylases
Author(s) -
Schärer Orlando D.,
Jiricny Josef
Publication year - 2001
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/1521-1878(200103)23:3<270::aid-bies1037>3.0.co;2-j
Subject(s) - dna glycosylase , uracil dna glycosylase , base excision repair , biology , dna , dna repair , computational biology , genetics , biochemistry
Since the discovery in 1974 of uracil DNA glycosylase (UDG), the first member of the family of enzymes involved in base excision repair (BER), considerable progress has been made in the understanding of DNA glycosylases, the polypeptides that remove damaged or mispaired DNA bases from DNA. We also know the enzymes that act downstream of the glycosylases, in the processing of abasic sites, in gap filling and in DNA ligation. This article covers the most recent developments in our understanding of BER, with particular emphasis on the mechanistic aspects of this process, which have been made possible by the elucidation of the crystal structures of several glycosylases in complex with their respective substrates, substrate analogues and products. The biological importance of individual BER pathways is also being appreciated through the inactivation of key BER genes in knockout mouse models. BioEssays 23:270–281, 2001. © 2001 John Wiley & Sons, Inc.