TY - JOUR
T1 - Repair of 8-hydroxyguanine in DNA by mammalian N-methylpurine-DNA glycosylase
AU - Bessho, Tadayoshi
AU - Roy, Rabindra
AU - Yamamoto, Kazuo
AU - Kasai, Hiroshi
AU - Nishimura, Susumu
AU - Tano, Keizo
AU - Mitra, Sankar
PY - 1993/10/1
Y1 - 1993/10/1
N2 - 8-Hydroxyguanine is one of the major base lesions implicated in mutagenesis induced by ionizing radiation and radiomimetic agents. This lesion appears to be repaired by human cells via multiple pathways including the one that involves a base glycosylase. Mouse N-methylpurine-DNA glycosylase, responsible for the removal of N-alkylpurines in DNA that are induced by simple monofunctional alkylating agents, also releases 8-hydroxyguanine from DNA in vitro and in vivo in Escherichia coli. The human N-methylpurine-DNA glycosylase, with a lower preference for N-alkylguanine than the mouse protein, removes the oxidized base less efficiently than the mouse protein. The recombinant mammalian glycosylases can rescue E. coli lacking MutM (Fpg) protein, the DNA glycosylase that is primarily responsible for removing 8-hydroxyguanine from the bacterial DNA.
AB - 8-Hydroxyguanine is one of the major base lesions implicated in mutagenesis induced by ionizing radiation and radiomimetic agents. This lesion appears to be repaired by human cells via multiple pathways including the one that involves a base glycosylase. Mouse N-methylpurine-DNA glycosylase, responsible for the removal of N-alkylpurines in DNA that are induced by simple monofunctional alkylating agents, also releases 8-hydroxyguanine from DNA in vitro and in vivo in Escherichia coli. The human N-methylpurine-DNA glycosylase, with a lower preference for N-alkylguanine than the mouse protein, removes the oxidized base less efficiently than the mouse protein. The recombinant mammalian glycosylases can rescue E. coli lacking MutM (Fpg) protein, the DNA glycosylase that is primarily responsible for removing 8-hydroxyguanine from the bacterial DNA.
KW - DNA repair
KW - Mutation suppression
KW - Oxidative DNA damage
UR - http://www.scopus.com/inward/record.url?scp=0027489205&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027489205&partnerID=8YFLogxK
U2 - 10.1073/pnas.90.19.8901
DO - 10.1073/pnas.90.19.8901
M3 - Article
C2 - 8415629
AN - SCOPUS:0027489205
SN - 0027-8424
VL - 90
SP - 8901
EP - 8904
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 19
ER -