Investigation of the specificity of O6-alkylguanine-DNA-alkyltransferase.
Comparison of the abilities of alkylated RNA and DNA to serve as substrates for the O6-alkylguanine-DNA-alkyltransferase have been carried out. It was found that the O6-methylguanine in tRNA was much less active as a substrate for the protein than O6-methylguanine in double stranded DNA. The difference in rates of repair was such that it is unlikely that the alkyltransferase would act on RNA in vivo and, therefore, the reaction with RNA should not contribute towards the exhaustion of its repair capacity.
Pegg
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Department of Physiology, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey 17033.
Morimoto
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Dolan
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D002851:Chromatography, High Pressure Liquid; D003110:Colonic Neoplasms / Q000201:enzymology; D004247:DNA / Q000378:metabolism; D004260:DNA Repair; D004926:Escherichia coli / Q000201:enzymology; D006147:Guanine / Q000031:analogs & derivatives / Q000378:metabolism; D006801:Humans; D008780:Methyltransferases / Q000378:metabolism*; D019853:O(6)-Methylguanine-DNA Methyltransferase; D012313:RNA / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured
D006147:Guanine; D012313:RNA; D004247:DNA; D012343:RNA, Transfer; C008449:O-(6)-methylguanine; D008780:Methyltransferases; D019853:O(6)-Methylguanine-DNA Methyltransferase