Characterization of the aldehyde reactive probe reaction with AP-sites in DNA: Influence of AP-lyase on adduct stability
Characterization of the aldehyde reactive probe reaction with AP-sites in DNA: Influence of AP-lyase on adduct stability
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DOI:
10.1080/15257770600726133
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发表时间:
2006-01-01
影响因子:
1.3
通讯作者:
Kitner, Joshua
中科院分区:
文献类型:
--
作者:
Bennett, Samuel E.;Kitner, Joshua
Alkoxyamines react with the open-chain aldehyde form of AP-sites in DNA to produce open-chain aldehyde oximes. Here we characterize the effect of AP-site cleavage by yeast AP-endonuclease 1 (APN1) or T4 pyrimidine dimer DNA glycosylase/AP-lyase (T4 Pdg) on the efficiency and stability of the alkoxyamine aldehyde reactive probe (APLP) condensation reaction with AP-sites. The results indicate that (1) reaction of APLP with the open-chain aldehyde equilibrium form of the AP-site was less efficient than with the 3'-alpha,beta-unsaturated aldehyde produced by T4 Pdg; (2) the dRP moiety was least reactive with ARP; (3) both the AP-site and 3'-alpha,beta-unsaturated aldehyde were stable with regard to reaction with APLP over a 30-min incubation period at 37 degrees C and (4) APLP adducted to the open-chain aldehyde form of the AP-site could be replaced by methoxyamine, but the 3'-alpha,beta-unsaturated aldehyde APLP oxime was stable against methoxyamine attack.