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3‐methyladenine DNA glycosylases: structure, function, and biological importance
Author(s) -
Wyatt Michael D.,
Allan James M.,
Lau Albert Y.,
Ellenberger Tom E.,
Samson Leona D.
Publication year - 1999
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/(sici)1521-1878(199908)21:8<668::aid-bies6>3.0.co;2-d
Subject(s) - dna glycosylase , dna , dna repair , dna damage , biology , enzyme , genome , base excision repair , function (biology) , computational biology , genetics , biochemistry , gene
The genome continuously suffers damage due to its reactivity with chemical and physical agents. Finding such damage in genomes (that can be several million to several billion nucleotide base pairs in size) is a seemingly daunting task. 3‐Methyladenine DNA glycosylases can initiate the base excision repair (BER) of an extraordinarily wide range of substrate bases. The advantage of such broad substrate recognition is that these enzymes provide resistance to a wide variety of DNA damaging agents; however, under certain circumstances, the eclectic nature of these enzymes can confer some biological disadvantages. Solving the X‐ray crystal structures of two 3‐methyladenine DNA glycosylases, and creating cells and animals altered for this activity, contributes to our understanding of their enzyme mechanism and how such enzymes influence the biological response of organisms to several different types of DNA damage. BioEssays 21:668–676, 1999. © 1999 John Wiley & Sons, Inc.