Nucleic Acids Research, Vol 27, Issue 11 2256-2264, Copyright © 1999 by Oxford University Press
AM Avery, B Kaur, JS Taylor, JA Mello, JM Essigmann and PW Doetsch
Schizosaccharomyces pombe ultraviolet DNA endonuclease (UVDE or Uve1p) has
been shown to cleave 5' to UV light-induced cyclobutane pyrimidine dimers
(CPDs) and pyrimidine-pyrimidone (6-4) photoproducts (6-4PP). This
endonuclease is believed to function in the initial step in an alternative
excision repair pathway for the removal of DNA damage caused by exposure to
UV light. An active truncated form of this protein, Delta228-Uve1p, has
been successfully overexpressed, affinity purified and partially
characterized. In the present study we present data from a detailed
substrate specificity trial. We have determined that the substrate range of
Uve1p is much greater than was originally believed. We demonstrate that
this DNA damage repair protein is capable of recognizing an array of
UV-induced DNA photoproducts (cis-syn-, trans-syn I- and trans-syn II CPDs,
6-4PP and Dewar isomers) that cause varying degrees of distortion in a
duplex DNA molecule. We also demonstrate that Uve1p recognizes
non-UV-induced DNA damage, such as platinum-DNA GG diadducts, uracil,
dihydrouracil and abasic sites. This is the first time that a single DNA
repair endonuclease with the ability to recognize such a diverse range of
lesions has been described. This study suggests that Uve1p and the
alternative excision repair pathway may participate broadly in the repair
of DNA damage.
ARTICLES
Substrate specificity of ultraviolet DNA endonuclease (UVDE/Uve1p) from Schizosaccharomyces pombe
Department of Biochemistry, Graduate Program in Biochemistry, Cell and Developmental Biology, Division of Cancer Biology, Emory University, School of Medicine, Atlanta, GA 30322, USA.
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