Nucleic Acids Research, Vol 27, Issue 4 979-983, Copyright © 1999 by Oxford University Press
T Bessho
An ionizing radiation-induced DNA lesion, thymine glycol, is removed from
DNA by a thymine glycol DNA glycosylase with an apurinic/apyrimidinic (AP)
lyase activity encoded by the Escherichia coli endonuclease III ( nth )
gene and its homolog in humans. Cells from Cockayne syndrome patients with
mutations in the XPG gene show approximately 2-fold reduced global repair
of thymine glycol. Hence, I decided to investigate the molecular mechanism
of the effect of XPG protein observed in vivo on thymine glycol removal by
studying the interactions of XPG protein and human endonuclease III (HsNTH)
protein in vitro and the effect of XPG protein on the activity of HsNTH
protein on a substrate containing thymine glycol. The XPG protein
stimulates the binding of HsNTH protein to its substrate and increases its
glycosylase/AP lyase activity by a factor of approximately 2 through direct
interaction between the two proteins. These results provide in vitro
evidence for a second function of XPG protein in DNA repair and a
mechanistic basis for its stimulatory activity on HsNTH protein.
ARTICLES
Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase
Department of Biochemistry and Biophysics, Mary Ellen Jones Building, CB 7260, University of North CarolinaSchool of Medicine, Chapel Hill, NC 27599-7260, USA. tbess@med.unc.edu
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