Nucleic Acids Research, Vol 26, Issue 22 5116-5122, Copyright © 1998 by Oxford University Press
TK Hazra, T Izumi, L Maidt, RA Floyd and S Mitra
8-Oxoguanine (8-oxoG), induced by reactive oxygen species (ROS) and
ionizing radiation, is arguably the most important mutagenic lesion in DNA.
This oxidized base, because of its mispairing with A, induces GC-- >TA
transversion mutations often observed spontaneously in tumor cells. The
human cDNA encoding the repair enzyme 8-oxoG-DNA glycosylase (OGG- 1) has
recently been cloned, however, its activity was never detected in cells.
Here we show that the apparent lack of this activity could be due to the
presence of an 8-oxoG-specific DNA binding protein. Moreover, we
demonstrate the presence of two antigenically distinct OGG activities with
an identical reaction mechanism in human cell (HeLa) extracts. The 38 kDa
OGG-1, identical to the cloned enzyme, cleaves 8- oxoG when paired with
cytosine, thymine and guanine but not adenine in DNA. In contrast, the
newly discovered 36 kDa OGG-2 prefers 8-oxoG paired with G and A. We
propose that OGG-1 and OGG-2 have distinct antimutagenic functions in vivo
. OGG-1 prevents mutation by removing 8- oxoG formed in DNA in situ and
paired with C, while OGG-2 removes 8- oxoG that is incorporated opposite A
in DNA from ROS-induced 8-oxodGTP. We predict that OGG-2 specifically
removes such 8-oxoG residues only from the nascent strand, possibly by
utilizing the same mechanism as the DNA mismatch repair pathway.
ARTICLES
The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutation
Sealy Center for Molecular Science and Department of Human Biological Chemistry and Genetics,University of Texas Medical Branch, Galveston, TX 77555.
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